MANNANASE FOR FORMULATIONS HAVING PH 5-12

Novel heparanase splice variant

The present invention, in at least some aspects, is of splice variants of heparanase, as well as diagnostic kits and methods of use, and therapeutic agents and methods of use based thereon, and antibodies specifically binding thereof.

Yeast strains producing mammalian-like complex n-glycans

Described herein are methods and genetically engineered fungal cells useful for producing target molecules containing mammalian-like complex N-glycans or containing intermediates in a mammalian glycosylation pathway.

PREBIOTIC OLIGOSACCHARIDES

The present invention provides galacto-oligosaccharide compositions that preferentially stimulate growth of specific species and subspecies. 1Bifidobacterium. A method for stimulating beneficial microflora in an animal , the method comprising ,{'i': 'Bifidobacterium', 'administering a sufficient amount of the composition of galacto-oligosaccharides, wherein at least 45% of the galacto-oligosaccharides by weight are tetra or penta galacto-oligosaccharides or wherein at least 25% of the galacto-oligosaccharides by weight are tetra galacto-oligosaccharides, to the animal to stimulate colonization of the gut of the animal by at least one beneficial strain.'}2Bifidobacterium breveBifidobacterium longuminfantis.. The method of claim 1 , wherein the composition further comprises or bv.3. The method of claim 1 , wherein the composition has less than 20% by weight of dimeric galacto-oligosaccharides claim 1 , based on weight of the total oligosaccharides.4. The method of claim 1 , wherein the composition has less than 10% by weight of dimeric galacto-oligosaccharides claim 1 , based on weight of the total oligosaccharides.5. The method of claim 1 , wherein the composition has less than 5% by weight of monomeric sugars based on total sugar and oligosaccharide solids.6. The method of claim 1 , wherein the composition has less than 5% by weight of lactose claim 1 , based on weight of the total oligosaccharides.7. The method of claim 1 , wherein the composition comprises a lactase enzyme.8. The method of claim 1 , wherein the composition is a food product or dietary supplement product.9. The method of claim 1 , wherein the food product is selected from the group consisting of an infant formula claim 1 , a follow-on formula claim 1 , and a toddler beverage.10. The method of claim 1 , wherein less than 10% of the galacto-oligosaccharides by weight have a degree of polymerization of 6 or greater.11. The method of claim 1 , wherein less than 10% of the galacto-oligosaccharides by ...

Compositions for Relieving the Symptoms of Gluten Sensitivity and Methods of Use Thereof

The disclosure relates to a composition that may be used to prevent the symptoms of non-celiac gluten sensitivity and may include ingredients that degrade or inactivate gluten and other components that may cause these symptoms. 1. A composition for reducing gluten sensitivity , comprising at least three proteases;at least one carbohydrase;at least one probiotic; andwherein said composition relieves symptoms of gluten sensitivity.2. The composition of further comprising ginger and turmeric.3. The composition of wherein said composition relieves the symptoms of non-celiac gluten sensitivity.4Aspergillus oryzaeAspergillus melleus. The composition of wherein said at least three proteases are selected from the group consisting of Protease 3.0 claim 1 , Protease 4.5 claim 1 , Protease 6.0 claim 1 , Papain claim 1 , Bromelain claim 1 , Protease claim 1 , Protease claim 1 , Proteases I-V claim 1 , and DPP IV and combinations thereof.5. The composition of wherein said at least one carbohydrase is selected from the group consisting of lactase claim 1 , α-galactosidase claim 1 , β-glucanase claim 1 , xylanase claim 1 , glucoamylase claim 1 , amylase claim 1 , hemicellulase claim 1 , invertase and pectinase and combinations thereof.6Lactococcus lactisLactococcus cremoris.. The composition of wherein said at least one probiotic is selected from the group consisting of and7. The composition of wherein said composition prevents the symptoms of non-celiac gluten sensitivity where said symptoms are selected from the group consisting of abdominal pain claim 1 , cramping claim 1 , bloating/distention claim 1 , diarrhea claim 1 , constipation and fatigue and combinations thereof.8. The composition of wherein said symptoms of non-celiac gluten sensitivity are selected from the group consisting of abdominal pain claim 7 , bloating claim 7 , changes in bowel habits and fatigue and combinations thereof.9. The composition of wherein said composition reduces the concentration of gluten to ...

Pichia pastoris surface display system

This disclosure relates to novel Pichia pastoris display systems, e.g., display systems featuring the Pichia pastoris strains (such as SuperMan5) with substantially homogeneous N-glycans displayed on cell surface proteins.

Polypeptides Having Protease Activity and Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having protease activity, and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. An isolated polypeptide having protease activity , selected from the group consisting of:(a) a polypeptide having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, or 100% sequence identity to the mature polypeptide of SEQ ID NO: 2, or the mature polypeptide of SEQ ID NO: 4 and(b) a polypeptide encoded by a polynucleotide having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 95.5%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, at least 99.5%, or 100% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1, or to the mature polypeptide coding sequence of SEQ ID NO: 3.2. The polypeptide of comprising or consisting of a) SEQ ID NO: 2 or the mature polypeptide of SEQ ID NO: 2 claim 1 , or b) SEQ ID NO: 4 or the mature polypeptide of SEQ ID NO: 4.3. The polypeptide of claim 2 , wherein the mature polypeptide is amino acids 1 to 313 of SEQ ID NO: 2 claim 2 , or amino acids 1 to 313 of SEQ ID NO: 4.4. The polypeptide of claim 1 , which is a variant of the mature polypeptide of SEQ ID NO: 2 or a variant of the mature polypeptide of SEQ ID NO: 4 comprising a substitution claim 1 , deletion claim 1 , and/or insertion at one or more positions.5. A composition comprising the polypeptide of .6. The composition of being a detergent composition such as a composition for laundry or automatic dish washing.7. The composition of further comprising one of more additional enzymes selected among claim 5 , proteases claim 5 , ...

Cellulolytic enzyme compositions and uses thereof

The present invention relates to recombinant filamentous fungal host cells producing cellulolytic enzyme compositions and methods of producing and using the compositions. 123-. (canceled)24Aspergillus fumigatusAspergillus fumigatusAspergillus fumigatusPenicillium. An enzyme composition comprising: (a) an cellobiohydrolase I; (b) an cellobiohydrolase II; (c) an beta-glucosidase or a variant thereof; and (d) a sp. GH61 polypeptide having cellulolytic enhancing activity; or homologs thereof;{'i': 'Aspergillus fumigatus', 'wherein the cellobiohydrolase I or homolog thereof is selected from the group consisting of(i) a cellobiohydrolase I comprising amino acids 27 to 532 of SEQ ID NO: 2;(ii) a cellobiohydrolase I comprising an amino acid sequence having at least 90% sequence identity to amino acids 27 to 532 of SEQ ID NO: 2;(iii) a cellobiohydrolase I encoded by a polynucleotide comprising a nucleotide sequence having at least 90% sequence identity to nucleotides 79 to 1596 of SEQ ID NO: 1; and(iv) a cellobiohydrolase I encoded by a polynucleotide that hybridizes under high stringency conditions with the full-length complement of nucleotides 79 to 1596 of SEQ ID NO: 1, wherein high stringency conditions are defined as prehybridization and hybridization at 42° C. in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon sperm DNA, and 50% formamide, and washing three times each for 15 minutes using 2×SSC, 0.2% SDS at 65° C.;{'i': 'Aspergillus fumigatus', 'wherein the cellobiohydrolase II or homolog thereof is selected from the group consisting of(i) a cellobiohydrolase II comprising amino acids 20 to 454 of SEQ ID NO: 4;(ii) a cellobiohydrolase II comprising an amino acid sequence having at least 90% sequence identity to amino acids 20 to 454 of SEQ ID NO: 4;(iii) a cellobiohydrolase II encoded by a polynucleotide comprising a nucleotide sequence having at least 90% sequence identity to nucleotides 58 to 1700 of SEQ ID NO: 3; and(iv) a cellobiohydrolase II ...

LACTASE-CONTAINING DOUBLE MICROCAPSULE, PREPARATION METHOD THEREFOR, AND USE THEREOF

The present invention provides a lactase-containing double microcapsule which includes; lactase provided as a core material; and a primary coating material and a secondary coating material, which are sequentially coated on the core material to be formulated, a method for preparing the lactase-containing double microcapsule, and a dairy product including the lactase-containing double microcapsule as a use of the lactase-containing double microcapsule. 1. A lactase-containing double microcapsule comprising: lactase provided as a core material; and a primary coating material and a secondary coating material , which are sequentially coated on the core material to be formulated.2. The lactase-containing double microcapsule according to claim 1 , wherein the primary coating material includes at least one selected from the group consisting of medium-chain triglyceride (MCT) claim 1 , hydrogenated corn oil claim 1 , soybean oil claim 1 , safflower seed oil and butter oil.3. The lactase-containing double microcapsule according to claim 1 , wherein the secondary coating material includes at least one selected from the group consisting of hydroxypropyl methylcellulose phthalate claim 1 , zein claim 1 , shellac claim 1 , Eudragit claim 1 , cellulose acetate phthalate claim 1 , cellulose acetate succinate claim 1 , polyvinyl acetate phthalate claim 1 , cellulose acetate trimellitate claim 1 , hypromellose acetate succinate and phenyl salicylate.4. The lactase-containing double microcapsule according to claim 1 , wherein the formulation is in any form selected from the group consisting of powders claim 1 , solution claim 1 , tablets claim 1 , and granules.5. A method for preparing lactase-containing double microcapsule comprising:providing lactase as a core material, and stirring the core material with a primary coating material and a primary emulsifier to obtain an emulsion of lactase;stirring the emulsion of lactase with secondary coating material and a secondary emulsifier ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND MAGNESIUM

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and magnesium or a salt or complex thereof. The invention also relates to the combination of a sulforaphane or a derivative thereof and magnesium or a salt or complex thereof. The invention also relates to the combination of a broccoli extract or powder and magnesium or a salt or complex thereof. The invention provides compositions and methods relating to these combinations.

Polypeptides Having Alpha-Glucuronidase Activity And Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having alpha-glucuronidase activity, catalytic domains and polynucleotides encoding the polypeptides, catalytic domains. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides or catalytic domains. 118-. (canceled)19. A nucleic acid construct comprising a polynucleotide encoding a polypeptide having alpha-glucuronidase activity , wherein the polynucleotide is operably linked to one or more heterologous control sequences that direct the production of the polypeptide in an expression host , and wherein the polypeptide having alpha-glucuronidase activity is selected from the group consisting of:(a) a polypeptide having at least 80% sequence identity to the mature polypeptide of SEQ ID NO: 6 or the mature polypeptide of SEQ ID NO: 8;(b) a polypeptide encoded by a polynucleotide that hybridizes under high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO:1, (ii) the cDNA sequence thereof, or (iii) the full-length complement of (i) or (ii), wherein high stringency conditions are defined as prehybridization and hybridization at 42° C. in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon sperm DNA, and 50% formamide, and washing three times each for 15 minutes using 2×SSC, 0.2% SDS at 65° C.; and(c) a polypeptide encoded by a polynucleotide having at least 80% sequence identity to the mature polypeptide coding sequence of SEQ ID NO:1 or the cDNA sequence thereof.20. The nucleic acid construct of claim 19 , wherein the polypeptide has at least 80% sequence identity to the mature polypeptide of SEQ ID NO: 6 or the mature polypeptide of SEQ ID NO: 8.21. The nucleic acid construct of claim 19 , wherein the polypeptide has at least 85% sequence identity to the mature polypeptide of SEQ ID NO: 6 or the mature polypeptide of SEQ ID NO: 8.22. The nucleic acid construct ...

Heparanase expression in human t lymphocytes

Embodiments of the present disclosure concern improvements to cell therapy for cancer. In certain embodiments, an ex vivo expanded T cell lacks endogenous heparanase expression, and amelioration of this effect allows an improvement for cancer cell therapy, including of solid tumors. In specific embodiments, ex vivo expanded T cells comprise recombinant heparanase expression.

ANIMAL CELL STRAIN AND METHOD FOR USE IN PRODUCING GLYCOPROTEIN, GLYCOPROTEIN AND USE THEREOF

Provided are an animal cell strain for use in producing a glycoprotein which uses a high-mannose sugar chain as a main N-glycan structure, a method for use in producing a glycoprotein by using the cell strain, a glycoprotein produced by using the method, and a use thereof. At least two genes from among a Golgi mannosidase and an endoplasmic reticulum mannosidase gene of the cell strain are damaged or knocked out. 1. An animal cell strain capable of producing a glycoprotein having a high-mannose type sugar chain as a main N-linked sugar chain structure , wherein at least two genes of the Golgi mannosidase and endoplasmic reticulum mannosidase genes in the cell strain are destroyed or knocked out.2. The animal cell strain according to claim 1 , wherein the high-mannose type sugar chain is at least one selected from the group consisting of Glc1-Man9-GlcNAc2 claim 1 , Man9-GlcNAc2 claim 1 , Man8-GlcNAc2 claim 1 , Man7-GlcNAc2 claim 1 , Man6-GlcNAc2 and Man5-GlcNAc2.3Xenopus. The animal cell strain according to claim 1 , wherein the cell strain is derived from a mammalian cell selected from the group consisting of human embryonic kidney cell (HEK293) claim 1 , Chinese hamster ovary cell (CHO) claim 1 , COS claim 1 , 3T3 claim 1 , myeloma claim 1 , BHK claim 1 , HeLa and Vero claim 1 , or an amphibian cell selected from the group consisting of egg cells or an insect cell Sf9 claim 1 , Sf21 or Tn5.4. The animal cell strain according to claim 3 , wherein the cell strain is derived from human embryonic kidney cell (HEK293) or Chinese hamster ovary cell (CHO).5. The animal cell strain according to claim 1 , whereinthe destroying is achieved by a gene-destroying method targeting a Golgi mannosidase gene and/or an endoplasmic reticulum mannosidase gene, and/orthe knockout is achieved by a gene knockout method targeting a Golgi mannosidase gene and/or an endoplasmic reticulum mannosidase gene.6. The animal cell strain according to claim 5 , wherein the endoplasmic reticulum ...

MUTANT ENDOGLYCOCERAMIDASES WITH ENHANCED SYNTHETIC ACTIVITY

The present invention relates to a novel endoglycoceramidase whose hydrolytic activity has been substantially reduced or eliminated, such that the enzyme is useful for synthesis of glycolipids from a monosaccharide or oligosaccharide and a ceramide. More specifically, the endoglycoceramidase is a mutant version of a naturally occurring endoglycoceramidase, preferably comprising a mutation within the active site or the nucleophilic site of the enzyme and more preferably comprising a substitution mutation of the Glu residue within the active site or the nucleophilic site. Also disclosed are a method for generating the mutant endoglycoceramidase and a method for enzymatically synthesizing glycolipids using this mutant enzyme. 1. (canceled)2. A mutant endoglycoceramidase , wherein the mutant endoglycoceramidase comprises a wild-type endoglycoceramidase peptide sequence including a nucleophilic region as set forth in SEQ ID NO: 54 modified by replacing a nucleophilic carboxylate amino acid residue of the nucleophilic region with a serine (Ser) , glycine (Gly) , or alanine (Ala) amino acid residue.3. The mutant endoglycoceramidase of claim 2 , wherein the mutant is capable of catalyzing the transfer of a saccharide moiety from a donor substrate to an acceptor substrate selected from a sphingosine claim 2 , a ceramide claim 2 , or an analog thereof claim 2 , thereby producing a glycolipid.4. The mutant endoglycoceramidase of claim 2 , wherein the corresponding wild-type endoglycoceramidase comprises an amino acid sequence set forth in SEQ ID NOs: 3 claim 2 , 6 claim 2 , 8 claim 2 , 11 claim 2 , 14 claim 2 , 17 claim 2 , 20 claim 2 , 23 claim 2 , 25 claim 2 , 26 claim 2 , 27 claim 2 , or 28.5. The mutant endoglycoceramidase of claim 2 , comprising any one of the amino acid sequences set forth in SEQ ID NOS: 55-66.6. A nucleic acid encoding the mutant endoglycoceramidase of .7. A vector comprising the nucleic acid of .8. A host cell comprising the nucleic acid of .9. A host ...

SULFORAPHANE/SULFORAPHANE PRECURSOR AND PHYTOSTEROL/PHYTOSTANOL COMPOSITIONS

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and a phytosterol and/or phytostanol or ester thereof. The invention also relates to the combination of a sulforaphane or a derivative thereof and a phytosterol and/or phytostanol or ester thereof. The invention also relates to the combination of a broccoli extract or powder and a phytosterol and/or phytostanol or ester thereof. The invention provides compositions and methods relating to these combinations. 1. An orally administrable composition comprising:a sulforaphane precursor;an enzyme capable of converting the sulforaphane precursor to sulforaphane;an enzyme potentiator; anda phytosterol and/or phytostanol or ester thereof.2. The orally administrable composition of claim 1 , wherein the sulforaphane precursor comprises glucoraphanin.3. The orally administrable composition of claim 1 , wherein the enzyme capable of converting the sulforaphane precursor to sulforaphane comprises myrosinase.4. The orally administrable composition of claim 1 , wherein the enzyme potentiator comprises ascorbic acid.5. The orally administrable composition of claim 1 , wherein the composition comprises an enteric-coated dosage form.6. The orally administrable composition of claim 1 , wherein the composition further comprises one or more additional components selected from the group consisting of: quercetin claim 1 , an aminosugar claim 1 , a glycosaminoglycan claim 1 , avocado/soybean unsaponifiables claim 1 , a vitamin claim 1 , coffee fruit claim 1 , magnesium claim 1 , ursolic acid claim 1 , a proanthocyanidin claim 1 , a catechin claim 1 , an alpha- or beta-glucan claim 1 , curcumin claim 1 , S-adenosylmethionine (SAMe) claim 1 , betalains claim 1 , lipoic acid claim 1 , gallic acid claim 1 , resveratrol claim 1 , hyaluronic acid claim 1 , boron claim 1 , methylsulfonylmethane (MSM) claim 1 , acetyl-keto-beta- ...

METHOD FOR ASSAYING ARYLSULFATASE ACTIVITY

A lactase preparation includes lactase and has a lactase activity of 4,000 NLU/g or more according to the FCC IV method, wherein the lactase originates from a lactase gene of yeast, and wherein the lactase preparation has an arylsulfatase activity of 0.1% or less based on the lactase activity, in which the arylsulfatase activity (unit: U/g) is determined and calculated. 115-. (canceled)16. A lactase preparation comprising lactase and having a lactase activity of 4 ,000 NLU/g or more according to the FCC IV method , wherein the lactase originates from a lactase gene of yeast , and wherein the lactase preparation has an arylsulfatase activity of 0.1% or less based on the lactase activity , in which the arylsulfatase activity (unit: U/g) is determined and calculated by a method comprising:(a) obtaining a sample by diluting the lactase preparation as a specimen in which the existence of the arylsulfatase is predicted with 100 mM potassium phosphate buffer (pH6.5) comprising 0.5M potassium chloride,(b) preparing an aqueous solution comprising potassium 4-methylumbelliferone sulfate in a concentration of 2 mM,(c) mixing the sample and the aqueous potassium 4-methylumbelliferone sulfate solution with each other at a ratio of 1:1 (volume basis) to react them at 37 degrees Celsius for 3 hours,(d) adding to the reacted solution, 0.1N aqueous sodium hydroxide solution having the same amount (volume basis) as that of the reacted solution to stop the reaction, thus obtaining a sample for determination,(e) determining fluorescence intensity at an excitation wavelength of 360 nm and a fluorescence wavelength of 450 nm,(f) preparing a plurality of 4-methylumbelliferone solutions with different 4-methylumbelliferone concentrations in 100 mM potassium phosphate buffer (pH6.5) comprising 0.5M potassium chloride, adding 0.1N aqueous sodium hydroxide solution to each of the plurality of 4-methylumbelliferone solutions in a similar way as in (d), and determining fluorescence intensities ...

Mutant Endoglycoceramidases with Enhanced Synthetic Activity

The present invention relates to a novel endoglycoceramidase whose hydrolytic activity has been substantially reduced or eliminated, such that the enzyme is useful for synthesis of glycolipids from a monosaccharide or oligosaccharide and a ceramide. More specifically, the endoglycoceramidase is a mutant version of a naturally occurring endoglycoceramidase, preferably comprising a mutation within the active site or the nucleophilic site of the enzyme and more preferably comprising a substitution mutation of the Glu residue within the active site or the nucleophilic site. Also disclosed are a method for generating the mutant endoglycoceramidase and a method for enzymatically synthesizing glycolipids using this mutant enzyme. 1. (canceled)2. A method of producing a glycolipid , the method comprising: contacting a donor substrate having an activated saccharide moiety and an acceptor substrate with a variant of a wild-type endoglycoceramidase in a reaction mixture , wherein the variant catalyzes the transfer of the saccharide moiety from the donor substrate to the acceptor substrate at a rate that exceeds hydrolysis of the glycolipid , wherein the wild-type endoglycoceramidase has a nucleophilic region comprising a (Ile/Met/Leu/Ph/Val)-(Leu/Met/Ile/Val)-(Gly/Ser/Thr)-(Glu/Asp)-(Phe/Thr/Met/Leu)-(Gly/Leu/Phe) sequence , said variant comprises an amino acid substitution of the Glu residue within said sequence in any one of SEQ ID NOs: 22 , 25 , 26 , 27 , and 28 wherein the amino acid substitution is selected from Ser , Gly , and Ala and wherein the acceptor substrate is sphingosine or a sphingosine analog.3. The method of claim 2 , further comprising: N-terminus (Met/Val/Leu)-Leu-Asp-(Met/Phe/Ala)-His-Gln-Asp-(Met/Val/Leu)-X-(Ser/Asn) SEQ ID NO: 50.4. The method of claim 3 , wherein said variant endoglycoceramidase exhibits increased catalytic activity in the transfer of the saccharide moiety from the donor substrate to the acceptor substrate as compared to the wild-type ...

METHOD FOR ASSAYING ARYLSULFATASE ACTIVITY

Provided is a method for determining activity of arylsulfatase in an aqueous system, which comprises a step in which arylsulfatase is subjected to reaction with a substrate, from which fluorophore or chromophore is liberated by suffering an action of the arylsulfatase, in an aqueous reaction system having high ionic strength. Also, provided are a lactase preparation having a lactase activity of 4,000 NLU/g or more according to the FCC IV method and having an arylsulfatase activity of 0.1% or less of the lactase activity as the basis, in which the arylsulfatase activity has been determined by the method for determining activity of arylsulfatase in an aqueous system according to the fluorescence method of the present invention; a method for producing this preparation; and a dairy product which comprises using this preparation. 113.-. (canceled)14. A method for producing a lactase preparation characterized by:culturing a diploid strain of yeast having a lactase gene, in which expression of arylsulfatase protein is restricted, or a gene-recombinant microorganism in which a lactase gene of yeast has been transformed and expression of arylsulfatase protein is restricted;gathering yeast or microorganism cells without destroying their cell walls, gathering culture fluid with yeast or microorganism cells after destruction of their cell walls, or gathering culture fluid without destroying cell walls; andpreparing a lactase preparation by using, as a raw material, the gathered yeast or microorganism cells and/or gathered culture fluid without a step for removing arylsulfatase;wherein the lactase preparation has a lactase activity of 4.000 NLU/a or more according to the FCC IV method; and (1) a specimen in which the existence of the arylsulfatase is predicted is arbitrarily diluted with 100 mM potassium phosphate buffer (pH6.5) comprising 0.5M potassium chloride to obtain a sample,', '(2) an aqueous solution comprising potassium 4-methylumbelliferone sulfate in a concentration ...

Cellobiohydrolase Variants and Polynucleotides Encoding Same

The present invention relates to cellobiohydrolase variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

Formulation of glucosinolates and myrosinase

A formulation includes microcapsules which contains a core containing an extract rich in glucosinolates obtained from crucifers and a biopolymer, and an enteric coating containing myrosinase and a biopolymer. A procedure is to obtain the same and to use the formulation as such, or in dietetic food supplements for humans or animals due to its immunostimulant activity.

HEMICELLULASE ENRICHED COMPOSITIONS FOR ENHANCING HYDROLYSIS OF BIOMASS

Described are compositions and methods relating to cellulase/hemicellulase enzyme blends for improving the enzymatic hydrolysis of cellulosic and hemicellulosic materials, as commonly found in biomass. 130-. (canceled)32Trichoderma reesei.. The method of claim 31 , wherein the hemicellulase composition comprises xylanase XYN2 from33. The method of claim 31 , wherein the hemicellulase composition further comprises at least one additional hemicellulase selected from the group consisting of a GH54 hemicellulase claim 31 , a GH62 hemicellulase claim 31 , a GH27 hemicellulase claim 31 , a GH36 hemicellulase claim 31 , a GH5 hemicellulase claim 31 , a GH74 hemicellulase claim 31 , a GH67 hemicellulase claim 31 , a GH28 hemicellulase claim 31 , a GH11 hemicellulase claim 31 , a GH10 hemicellulase claim 31 , a GH3 hemicellulase claim 31 , and a CE5 hemicellulase.34Trichoderma reeseiTrichoderma reesei.. The method of claim 31 , wherein the β-xylosidase is BXL1 from and the arabinofuranosidase is ABF1 claim 31 , ABF2 claim 31 , or ABF3 from35. The method of claim 31 , wherein contacting the mixture of cellulosic and hemicellulosic materials with the whole cellulase composition and the hemicellulase composition is performed simultaneously.36. The method of claim 31 , wherein contacting the mixture of cellulosic and hemicellulosic materials with the whole cellulase composition and the hemicellulase composition is performed sequentially.37. The method of claim 31 , wherein the whole cellulase composition and the hemicellulase composition are provided in a single composition enzyme blend.38. The method of claim 31 , wherein the mixture of cellulosic and hemicellulosic materials comprises one or more materials selected from the group consisting of wood claim 31 , wood pulp claim 31 , papermaking sludge claim 31 , paper pulp waste streams claim 31 , particle board claim 31 , corn stover claim 31 , corn fiber claim 31 , rice claim 31 , paper and pulp processing waste claim 31 , ...

Compositions and Methods for Modulating Growth of a Genetically Modified Gut Bacterial Cell

Compositions and methods are provided for modulating growth of a genetically modified bacterial cell present in a human organ, for modulating growth of a genetically modified bacterial cell in an organ (e.g., gut), for displacing at least a portion of a population of bacterial cells in an organ, and for facilitating gut colonization by a genetically modified bacterial cell. Also provided are genetically modified bacterial cells, e.g., cells that include a heterologous carbohydrate-utilization gene or gene set that provides for the ability to utilize as a carbon source a rare carbohydrate of interest that is utilized as a carbon source by less than 50% of bacterial cells present in a human microbiome. 1Bacteroides. A method of colonizing the gut of a subject with a genetically modified , non-naturally occurring cell , the method comprising administering to the subject both:{'i': Bacteroides', 'Bacteroides', 'Bacteroides, 'a) the genetically modified cell, wherein the genetically modified cell comprises a heterologous carbohydrate-utilization gene set that provides the genetically modified cell with an ability to utilize as a carbon source a porphyran and comprises at least twelve genes and one or more nucleic acids encoding a porphyranase; and'}b) porphyran.2B. plebeiusB. ovatus. The method of claim 1 , wherein the carbohydrate-utilization gene set comprises one or more nucleic acids encoding a porphyranase from the or genome.3. The method of claim 1 , wherein one of the nucleic acids encodes a protein having 80% or more sequence identity to SEQ ID NO: 19.4. The method of claim 1 , wherein one of the nucleic acids encodes a protein having 80% or more sequence identity to SEQ ID NO: 21.5. The method of claim 1 , wherein the carbohydrate-utilization gene set comprises one or more nucleic acids each selected from the group consisting of nucleic acids encoding a protein having 80% or more sequence identity to SEQ ID NOs: 14-34.6. The method claim 1 , wherein the ...

Baking lipase

Lipase enzymes and methods of using the lipases in a baking for improving the volume, stability, tolerance of a baked product and/or reducing and reducing or eliminating the use of DATEM.

COMPOSITIONS AND METHODS FOR MODULATING GROWTH OF A GENETICALLY MODIFIED GUT BACTERIAL CELL

Compositions and methods are provided for modulating growth of a genetically modified bacterial cell present in a human organ, for modulating growth of a genetically modified bacterial cell in an organ (e.g., gut), for displacing at least a portion of a population of bacterial cells in an organ, and for facilitating gut colonization by a genetically modified bacterial cell. Also provided are genetically modified bacterial cells, e.g., cells that include a heterologous carbohydrate-utilization gene or gene set that provides for the ability to utilize as a carbon source a rare carbohydrate of interest that is utilized as a carbon source by less than 50% of bacterial cells present in a human microbiome. 1Bacteroides. A genetically modified cell comprising:{'i': 'Bacteroides', 'a heterologous carbohydrate-utilization gene or gene set that provides the genetically modified cell with an ability to utilize as a carbon source a porphyran,'}wherein the heterologous carbohydrate-utilization gene or gene set comprises one or more nucleic acids encoding a porphyranase.2BacteroidesB. plebeiusB. ovatus. The genetically modified cell of claim 1 , wherein the heterologous carbohydrate-utilization gene or gene set comprises one or more nucleic acids encoding a porphyranase from the or genome.3Bacteroides. The genetically modified cell of claim 1 , wherein one of the nucleic acids encodes a protein having 80% or more sequence identity to SEQ ID NO: 19.4Bacteroides. The genetically modified cell of claim 1 , wherein one of the nucleic acids encodes a protein having 80% or more sequence identity to SEQ ID NO: 21.5BacteroidesBacteroides. The genetically modified cell of claim 1 , wherein the cell comprises the heterologous carbohydrate-utilization gene set.6Bacteroides. The genetically modified cell of claim 5 , wherein the carbohydrate-utilization gene set comprises at least twelve genes.7Bacteroides. The genetically modified cell of claim 5 , wherein the carbohydrate-utilization gene ...

Method for the Production of Xylobiose and Other Defined Xylooligosaccharides

The present invention provides compositions, methods, and kits based on a novel two-enzyme system. This system uses a combination of an appendage dependent endoxylanase and xylobiohydrolase activity to produce xylobiose and xylan-derived oligosaccharides using lignocellulosic biomass material, an enriched xylan fraction thereof, or an extracted, purified xylan material as a starting material. 1. A composition for the production of xylobiose and defined aldouronates , the composition comprising:a) an isolated appendage dependent endoxylanase; andb) an isolated xylobiohydrolase comprising an amino acid sequence with at least 90% identity to a sequence selected from the group consisting of SEQ ID NO:1-13 or a portion thereof with xylobiohydrolase activity.2. The composition of claim 1 , further comprising:c) a lignocellulosic biomass material, an enriched xylan fraction thereof, or an extracted, purified xylan material.3. The composition of claim 2 , wherein the lignocellulosic biomass material is pulped.4. The composition of claim 2 , wherein the lignocellulosic biomass material is derived from hardwood claim 2 , softwood claim 2 , or grass.5. The composition of claim 2 , wherein the lignocellulosic biomass material comprises glucuronoxylans and/or glucuronoarabinoxylans.6. The composition of claim 1 , wherein the isolated appendage dependent endoxylanase is a canonical glycoside hydrolase family 30 subfamily 8 (GH30-8) enzyme having at least 90% identity to a sequence selected from the group consisting of SEQ ID NO:14-18.7. The composition of further comprising an additional enzyme that is different than the isolated appendage dependent endoxylanase.8. The composition of claim 7 , wherein the additional enzyme is selected from arabinofuranosidases claim 7 , arabinoxylanases claim 7 , β-xylosidases claim 7 , α-glucuronidases claim 7 , and a GH30-8 enzyme.9. A method for producing xylobiose claim 7 , the method comprising contacting a lignocellulosic biomass material ...

Simplified Process For Producing Maltodextrin and Specialty Syrups

Disclosed are compositions and methods relating to a simplified process for producing maltodextrin and specialty syrups using fewer enzymes and less complicated conditions than required for contemporary enzymatic processes. 1. A method for producing a maltodextrin and/or a specialty syrup comprising contacting a starch substrate with an α-amylase (EC 3.2.1.1) capable of producing , in the substantial absence of a maltogenic enzyme selected from the group consisting of maltogenic amylase (EC 3.2.1.133) , β-amylase (EC 3.2.1.2) , pullulanase (EC 3.2.1.41) , glucoamylase (EC 3.2.1.3) and combinations , thereof , a syrup comprising a DE profile equivalent to the DE profile produced by conventional , multi-enzyme , acid pretreatment conditions that includes a maltogenic enzyme , wherein the method substantially obviates at least one pH adjustment or temperature adjustment step in an otherwise identical process utilizing a different , conventional liquifying α-amylase.2. The method of claim 1 , performed in the absence of a maltogenic enzyme claim 1 , with the exception of the α-amylase claim 1 , which may have maltogentic amylase activity.3. The method of claim 2 , performed in the absence of any maltogenic enzyme claim 2 , with the exception of the α-amylase claim 2 , which may have maltogentic amylase activity.4. The method of any of - claim 2 , wherein the process step is selected from the group consisting of reducing the pH of a liquefact to inactivate a different claim 2 , conventional liquifying α-amylase claim 2 , cooling the liquefact to promote optimal performance of a maltogenic enzyme claim 2 , heating a saccharified liquifact to inactivate the maltogenic enzyme claim 2 , and cooling the saccharified liquifact to concentrate the product.5Cytophaga. The method of any of - claim 2 , wherein the α-amylase is from a sp.6Cytophaga. The method of any of - claim 2 , wherein the α-amylase is the α-amylase from sp. having the amino acid sequence of SEQ ID NO: 1 claim 2 ...

Method of Preparing a Dough-Based Product

Dough with a high sucrose content (such as cake dough) tends to inhibit the activity of an anti-staling amylase such as Novamyl, making it less effective to prevent the staling of dough-based products with high sucrose content such as cakes. A good anti-staling effect in cakes can be achieved by using a carefully selected anti-staling amylase with certain properties. 1. A method of preparing a dough or a dough-based edible product , comprising adding a polypeptide to the dough , wherein the dough comprises at least 10% sucrose by weight , and the polypeptide:a) has an amino acid sequence which is at least 70% identical to SEQ ID NO: 1, andb) compared to SEQ ID NO: 1 comprises an amino acid alteration which is substitution or deletion of or insertion adjacent to I15, R18, K44, N86, T87, G88, Y89, H90, Y92, W93, F188, T189, D190, P191, A192, F194, L196, D329, N371, D372, P373, N375 or R376.2. The method of wherein the alteration is substitution with a larger or smaller amino acid residue.3. The method of wherein the alteration is insertion of 1-4 amino acid residues at the N- or C-side of the specified residue.4. The method of wherein the polypeptide comprises a substitution I15T/S/V/L claim 1 , R18K claim 1 , K44R/S/T/Q/N claim 1 , N86Q/S/T claim 1 , T87N/Q/S claim 1 , G88A/S/T claim 1 , Y89W/F/H claim 1 , H90W/F/Y/R/K/N/Q/M claim 1 , W93Y/F/M/E/G/V/T/S claim 1 , F188 H/L/I/T/G/V claim 1 , D190E/Q/G claim 1 , A192G/S/T/Q/R claim 1 , F194S/L/Y claim 1 , L196F claim 1 , N371K/R/F/Y/Q or D372E/Q/S/T/A claim 1 , a deletion of 191 or 192 or an insertion of Ala after 192.6. A method of preparing dough or a dough-based edible product claim 1 , comprising adding an exo-amylase to dough wherein the dough comprises at least 10% sucrose by weight claim 1 , and the exo-amylase has amylase activity in the presence of 10% sucrose by weight which is more than 20% of the activity without sucrose.7. The method of the preceding claim wherein the exo-amylase retains at least 20% ( ...

METHOD FOR PRODUCING LACTASE-CONTAINING COMPOSITION

A method for producing a lactase-containing composition which is purified by selectively removing protease contaminating the lactase using simple and easy means; a lactase-containing composition; and a dairy product containing the lactase-containing composition. 1. A method for producing a lactase-comprising composition having a reduced protease content , the method comprising:dissolving a composition comprising lactase and protease in an aqueous salt solution having an electric conductivity of from 2 to 45 mS/cm to obtain a resultant solution;bringing the resultant solution into contact with an ion exchange resin; andcollecting a fraction which is not adsorbed onto the ion exchange resin.2. The production method according to claim 1 , whereinthe composition comprising lactase and protease is a lactase-comprising composition produced by a microorganism.3. The production method according to claim 1 , whereinthe aqueous salt solution is an aqueous solution of an inorganic acid salt.4. The production method according to claim 1 , whereinthe ion exchange resin is an anion exchange resin.5. The production method according to claim 1 , whereinthe ion exchange resin is an anion exchange resin membrane.6. The production method according to claim 1 , whereinthe lactase-comprising composition having a reduced protease content has a ratio of protease activity to lactase activity of not more than 0.02%.7. A lactase-comprising composition claim 1 , which has a ratio of protease activity to lactase activity of not more than 0.02%.8. A lactase-comprising composition claim 1 , obtained by the method according to claim 1 ,wherein the lactase-comprising composition has a ratio of protease activity to lactase activity of not more than 0.02%.9. The lactase-comprising composition according to claim 7 , whereinfor a processed milk obtained by allowing milk to comprise 0.1 mass % of the lactase-comprising composition and to stand still at 30° C. for 3 months,when the processed milk is ...

SPECIAL ENZYME FOR GALACTOOLIGOSACCHARIDE PRODUCTION AS WELL AS PREPARATION AND APPLICATION THEREOF

A method of using lactase for generating galactooligosaccharide as well as the preparation and an application of the lactase are provided. Lactase (BglD305 derived from B2301 and BglD derived from ATCC 31382) molecules from two sources are taken as the basis for molecular evolution, so as to obtain new lactase enzyme molecules with high galactooligosaccharide synthesis efficiency and good expression performance. The high-producing strain lactase is further constructed, the lactase can be efficiently synthesized during the submerged fermentation, and the enzyme molecule is secreted into the culture medium, the high-activity enzyme preparation is directly prepared from the fermentation supernatant, and the lactase expression level can achieve 2208 U/mL. As the result, the fermentation manufacturing cost of lactase is reduced, the fermentation manufacturing process is simplified, and the quality of the lactase preparation is improved. 1. A lactase , wherein an amino acid sequence of the lactase is selected from the group consisting of SEQ ID NOS: 2 , 4 , 6 , 8 , 10 , 12 , 14 , 16 and 18.2. An encoding gene of the lactase of claim 1 , wherein the encoding gene of the lactase is selected from the group consisting of SEQ ID NOS: 1 claim 1 , 3 claim 1 , 5 claim 1 , 7 claim 1 , 9 claim 1 , 11 claim 1 , 13 claim 1 , 15 and 17.3. A recombinant vector or a recombinant strain claim 2 , comprising the encoding gene of the lactase of .4. The recombinant vector or the recombinant strain of claim 3 , wherein claim 3 , an expression vector used for the recombinant vector comprises:pHY-WZX, pBL-WZX, pHY300plk, pUB110, pE194, pHT1469, pWH1520, pHSE-001, pHSE-002, pHSE-003, pHSE-004, pHSE-005, pHSE-006, pHSE-007, pHSE-008, pHSE-009, pHSE-010, pHSE-011, pHSE-012, pHSE-013, pHSE-014, pHSE-015, pHSE-016, pHSE-017, or pHSE-018.5Bacillus licheniformis. The recombinant vector or the recombinant strain of claim 3 , wherein claim 3 , the expression vector pHSE-018 is a backbone of the ...

Process for Improving Freshness of Flat Breads Involving Combination of Maltogenic Alpha Amylase Variants

A method for improving the freshness of flat breads comprising a) adding to flour or to a dough comprising a flour, a first maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, and F188L; and a second maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, F194Y, and N375S; and b) making flat breads from the dough. 1. A method for improving the freshness of flat breads comprising 'a second maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, F194Y, and N375S; and', 'a) adding to flour or to a dough comprising a flour, a first maltogenic alpha-amylase having at least 70% identity to SEQ ID NO: 1, and compared to SEQ ID NO: 1 comprising the substitutions D261G, T288P, and F188L; and'}b) making flat breads from the dough.2. The method according to claim 1 , wherein the flat breads are baked.3. The method according to claim 1 , wherein the flour is selected from the group consisting of wheat flour claim 1 , corn flour claim 1 , rye flour claim 1 , barley flour claim 1 , oat flour claim 1 , rice flour claim 1 , sorghum flour claim 1 , soy flour claim 1 , flour from pulses like gram flour claim 1 , and any combination thereof.4. The method according to claim 1 , wherein the flat breads are selected from the group consisting of pita claim 1 , Arabic pita claim 1 , baladi claim 1 , Lebanese claim 1 , mafrood claim 1 , shami claim 1 , hapati claim 1 , sangak claim 1 , roti claim 1 , tortillas claim 1 , barbari claim 1 , nan claim 1 , taboon claim 1 , shrak claim 1 , mashrouh claim 1 , nasir claim 1 , tannoor claim 1 , lavash claim 1 , taftan claim 1 , chapatti claim 1 , and pizza.5. The method according to claim 1 , wherein the first maltogenic alpha-amylase has at least 75% claim 1 , 80% claim 1 , 85% claim 1 , ...

CELLULOLYTIC ENZYME COMPOSITIONS AND USES THEREOF

The present invention relates to recombinant filamentous fungal host cells producing cellulolytic enzyme compositions and methods of producing and using the compositions. 123-. (canceled)24Aspergillus fumigatusAspergillus fumigatusTrichoderma reesei. An enzyme composition , comprising: (i) an cellobiohydrolase I; (ii) an beta-glucosidase or variant thereof; and (iii); a endoglucanase; or homologs thereof.25Aspergillus fumigatus. The enzyme composition of claim 24 , wherein the cellobiohydrolase I or homolog thereof is selected from the group consisting of:(i) a cellobiohydrolase I comprising or consisting of the mature polypeptide of SEQ ID NO: 2;(ii) a cellobiohydrolase I comprising or consisting of an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the mature polypeptide of SEQ ID NO: 2;(iii) a cellobiohydrolase I encoded by a polynucleotide comprising or consisting of a nucleotide sequence having at least 70%, at least 75%, at least 80%, at least 81%, at least 82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1; and(iv) a cellobiohydrolase I encoded by a polynucleotide that hybridizes under at least high stringency conditions, very high stringency conditions, with the mature polypeptide coding sequence of SEQ ID NO: 1 or the full-length complement thereof;{'i': 'Aspergillus fumigatus', '#text': 'wherein the beta-glucosidase or homolog thereof is selected from the group consisting of:'}(i) a beta ...

THERMOSTABLE C. BESCII ENZYMES

The disclosure provides thermostable enzymes isolated from and fragments thereof useful for the degradation of cellulose and/or hemicellulose, including thermostable cellulases and hemicellulases. The disclosure further provides nucleic acids encoding the thermostable enzymes of the disclosure. The disclosure also provides methods for the conversion of cellulose and hemicellulose into fermentable sugars using thermostable enzymes of the disclosure. The disclosure also provides enzyme cocktails containing multiple enzymes disclosed herein. The enzymes can be used to release sugars present in cellulose or hemicellulose for subsequent fermentation to produce value-added products. 184-. (canceled)85. A host cell comprising two or more recombinant nucleic acids selected from the group consisting of:{'i': 'Caldicellulosiruptor bescii', 'a) a nucleic acid encoding the polypeptide of SEQ ID NO: 3 [endoxylanase (Cb193)],'}{'i': 'Caldicellulosiruptor bescii', 'b) a nucleic acid encoding the polypeptide of SEQ ID NO: 7 [endoxylanase (Cb195)],'}{'i': 'Caldicellulosiruptor bescii', 'c) a nucleic acid encoding the polypeptide of SEQ ID NO: 13 [α-arabinofuranosidase (Cb1172)],'}{'i': 'Caldicellulosiruptor bescii', 'd) a nucleic acid encoding the polypeptide of SEQ ID NO: 19 [α-glucuronidase (Cb909)],'}{'i': 'Caldicellulosiruptor bescii', 'e) a nucleic acid encoding the polypeptide of SEQ ID NO: 27 [β-xylosidase (Cb2487)],'}{'i': 'Caldicellulosiruptor bescii', 'f) a nucleic acid encoding the polypeptide of SEQ ID NO: 33 [acetyl xylan esterase (Cb162)], and'}{'i': 'Caldicellulosiruptor bescii', 'g) a nucleic acid encoding the polypeptide of SEQ ID NO: 37 [endoxylanase (Cb193) lacking signal peptide].'}86. A method for producing at least two of the enzymes selected from the group consisting of endoxylanase claim 85 , α-arabinofuranosidase claim 85 , α-glucuronidase claim 85 , β-xylosidase claim 85 , and acetyl xylan esterase claim 85 , comprising: culturing the host cell of in a ...

Method for reducing lactose at high temperatures

This specification relates to a method for reducing the amount of lactose in a milk-based substrate containing lactose, wherein said method comprises contacting said substrate with an enzyme having neutral lactase activity at a temperature of more than about 50° C., and wherein said lactase reduces the amount of lactose in said substrate by at least about 70%.

Compositions and methods for modulating growth of a genetically modified gut bacterial cell

Compositions and methods are provided for modulating growth of a genetically modified bacterial cell present in a human organ, for modulating growth of a genetically modified bacterial cell in an organ (e.g., gut), for displacing at least a portion of a population of bacterial cells in an organ, and for facilitating gut colonization by a genetically modified bacterial cell. Also provided are genetically modified bacterial cells, e.g., cells that include a heterologous carbohydrate-utilization gene or gene set that provides for the ability to utilize as a carbon source a rare carbohydrate of interest that is utilized as a carbon source by less than 50% of bacterial cells present in a human microbiome.

COMPOSITION OF DIGESTIVE ENZYMES AND APPETITE SUPPRESSANTS

The present invention relates to a composition, particularly a composition comprising digestive enzymes and appetite suppressant. The composition can be used for reducing appetite, inducing weight loss and/or promote food digestion in a subject in need thereof. 1. A composition comprising a digestive enzyme and an appetite suppressant.2. The composition of claim 1 , wherein the digestive enzyme is selected from the group consisting of protease claim 1 , lipase claim 1 , amylase claim 1 , invertase claim 1 , lactase claim 1 , cellulase claim 1 , xylanase claim 1 , aspergillopepsin claim 1 , α-galactosidase claim 1 , β-Glucanase claim 1 , glucoamylase claim 1 , pectinase claim 1 , peptidase claim 1 , aminopeptidase claim 1 , cholecystokinin claim 1 , secretin claim 1 , sucrase claim 1 , maltase claim 1 , isomaltase claim 1 , elastase claim 1 , trypsin claim 1 , chymotrypsin claim 1 , nuclease claim 1 , phospholipase claim 1 , pepsin claim 1 , and lysozyme.3. The composition of claim 1 , wherein the digestive enzyme is further coated with a polymer selected from the group consisting of cellulose acetate phthalate claim 1 , hydroxypropylmethylcellulose phthalate claim 1 , hydroxypropylmethylcellulose acetate succinate claim 1 , shellac claim 1 , acrylic acid polymer claim 1 , methacrylic acid polymer claim 1 , and methacrylic acid/methylmethacrylate copolymer.4. The composition of claim 1 , wherein the appetite suppressant is selected from the group consisting of naringin claim 1 , saffron extract claim 1 , green tea extract claim 1 , garcinia cambogia claim 1 , 5-HTP claim 1 , capsaicin claim 1 , black pepper or black pepper extract claim 1 , turmeric claim 1 , ginger or ginger extract and cinnamon.5. The composition of claim 1 , further comprising a stabilizer selected from the group consisting of proline claim 1 , trehalose claim 1 , dextran claim 1 , maltose claim 1 , sucrose claim 1 , mannitol claim 1 , polyols claim 1 , silica gel claim 1 , aminoguanidine claim 1 ...

CELL-ASSOCIATED HETEROLOGOUS FOOD AND/OR FEED ENZYMES

The present disclosure concerns recombinant yeast host cells expressing cell-associated heterologous food and/or feed enzymes which are expressed during the propagation phase of the recombinant yeast hosts cells. The recombinant yeast host cells can be used in a subsequent production process to make food and/or feed products, for example, baked products. 1. A recombinant yeast host cell having an heterologous nucleic acid molecule encoding a cell-associated heterologous food and/or feed enzyme , wherein the heterologous nucleic acid molecule is operatively associated with an heterologous promoter allowing the expression of the heterologous nucleic acid molecule during propagation.2. The recombinant yeast host cell of claim 1 , wherein the heterologous nucleic acid molecule allows the intracellular expression of the heterologous food and/or feed enzyme.3. The recombinant yeast host cell of claim 1 , wherein the heterologous nucleic acid molecule allows the expression of a membrane-associated heterologous food and/or feed enzyme.4. The recombinant yeast host cell of claim 3 , wherein the heterologous nucleic acid molecule allows the expression of a tethered heterologous food and/or feed enzyme.5. The recombinant yeast host cell of claim 4 , wherein the tethered heterologous food and/or feed enzyme is a chimeric protein of formula (I) or (II):{'br': None, 'sub': '2', '(NH)FFE-L-TT(COOH)\u2003\u2003(I)'}{'br': None, 'sub': '2', '(NH)TT-L-FFE(COOH)\u2003\u2003(II)'} L is present or absent and is an amino acid linker;', 'TT is an amino acid tethering moiety for associating the food and/or feed enzyme to a cell wall of the recombinant yeast host cell;', {'sub': '2', '(NH) indicates the amino terminus of the chimeric protein;'}, '(COOH) indicates the carboxyl terminus of the chimeric protein; and', '“-” is an amide linkage., 'wherein FFE is the food and/or feed enzyme;'}6. The recombinant yeast host cell of any one of to claim 4 , wherein the heterologous nucleic acid ...

OLIGO-SACCHARIDE ENHANCED MILK PRODUCTS HAVING THE FUNCTIONS OF MODULATING BLOOD LIPID, IMPROVING INTESTINAL FLORA AND PROMOTING IMMUNITY, AND PROCESS FOR PREPARING THE SAME

The subject invention aims to solve the problem of production of glucose accompanying the production of galactooligosaccharides after milk raw material is treated with lactase, by additionally adding transglucosidase to convert glucose to functional isomalto-oligosaccharide. The subject invention relates to a process for the production of a milk product enhanced with oligo-saccharides, characterized in that lactase and transglucosidase are used to treat milk raw materials. The subject invention further relates to the milk product of the process of the invention, whose oligo-saccharide content reaches a functional level. Human physiological effect assays confirm that the milk product increases intestinal probiotics, reduces harmful intestinal bacteria, improves the intestinal bacterial flora, reduces blood total cholesterol, reduces blood LDL cholesterol, increases blood HDL cholesterol, and improves the immunity, and may be used as low glycemic index (GI) dietary supplements. 1. A process for the production of a milk product enriched with oligosaccharides , comprising treating milk raw materials with lactase and transglucosidase.2. The process according to claim 1 , wherein the milk raw materials are cow milk claim 1 , goat milk or sheep milk.3. The process according to claim 1 , wherein the milk raw materials comprise about 10 to 60% (w/w) solid.4. The process according to claim 1 , comprising the following steps:(1) providing the milk raw materials;(2) adding about 0.01 to 0.5% (w/w) lactase and about 0.01 to 1.0% (w/w) transglucosidase to the milk raw materials; and(3) reacting at about 40 to 60° C. for about 30 to 90 minutes.5. The process according to claim 4 , wherein the milk raw materials are milk that comprises about 10% to about 60% (w/w) solid.6KluyveromycesAspergillus.. The process according to claim 4 , wherein the lactase is from and the transglucosidase is from7. The process according to claim 4 , wherein step (3) reacts at about 50° C. for about 60 ...

Glycosidase regimen for treatment of infectious disease

In various aspects, the invention relates to immune tolerant glycosidase therapy. The invention provides methods for treating or preventing infectious disease, including chronic viral infections, and highly contagious infectious agents that present an ongoing challenge for the immune system. The compositions and treatment regimens find use with other antiviral or antimicrobial therapies, as well as in conjunction with vaccination to boost effectiveness and/or extend the duration of protective effect. In certain embodiments, the regimen described herein reduces or eliminates the need for administration of other traditional antiviral or antimicrobial therapies. In various embodiments, the invention finds use in immunocompromised patients to boost immune function.

PICHIA PASTORIS STRAINS FOR PRODUCING PREDOMINANTLY HOMOGENEOUS GLYCAN STRUCTURE

Disclosed herein are novel strains for expression of exogenous proteins with substantially homogeneous N-glycans. The strains are genetically engineered to include a mutant OCH1 allele which is transcribed into an mRNA coding for a mutant OCH1 gene product (i.e., α-1,6-mannosyltransferase, or “OCH1 protein”). The mutant OCH1 protein contains a catalytic domain substantially identical to that of the wild type OCH1 protein, but lacks an N-terminal sequence necessary to target the OCH1 protein to the Golgi apparatus. The strains disclosed herein are robust, stable, and transformable, and the mutant OCH1 allele and the ability to produce substantially homogeneous N-glycans are maintained for generations after rounds of freezing and thawing and after subsequent transformations. 1Pichia pastoris. An engineered stable strain of , comprising:a mutant OCH1 allele which is transcribed into a mRNA coding for a mutant OCH1 protein that comprises a catalytic domain substantially identical with that of the wild type OCH1 protein, and an N-terminal sequence that alters the Golgi localization of the mutant OCH1 protein as compared to the wild type OCH1 protein, wherein said strain produce substantially homogeneous N-glycans.2. The strain of claim 1 , wherein the C-terminal fragment of the mutant OCH1 protein comprising the catalytic domain is at least 95% identical with amino acids 45-404 of SEQ ID NO: 2.3. The strain of claim 1 , wherein said mutant OCH1 protein lacks an N-terminal sequence for targeting the mutant OCH1 protein to the Golgi apparatus.4. The strain of claim 3 , wherein the mutant OCH1 protein lacks a membrane anchor domain at the N-terminal region.5. The strain of claim 1 , wherein the lack of a membrane anchor domain in the mutant OCH1 protein is a result of deletion of an N-terminal portion of the OCH1 wild type protein claim 1 , wherein the deleted portion comprises one or more amino acids of the membrane anchor domain of the wild type OCH1 protein.6. The strain ...

METHODS AND KITS FOR ASSAYING ENDOGLYCOSIDASE ACTIVITY

A method for assaying endoglycosidase activity includes providing a proteoglycan having a glycosaminoglycan chain with a non-reducing end; treating the proteoglycan with a glycosyltransferase to incorporate a carbohydrate into the non-reducing end of the glycosaminoglycan chain, wherein the carbohydrate includes a click chemistry moiety; adding a label to the proteoglycan, wherein the label includes a click chemistry moiety that reacts to the click chemistry moiety of the carbohydrate such that the label attaches to the carbohydrate to form a labeled proteoglycan; immobilizing the labeled proteoglycan on a multi-well plate, wherein the multi-well plate includes a specific anti-proteoglycan antibody for binding the labeled proteoglycan; treating the labeled proteoglycan with an endoglycosidase specific to the glycosaminoglycan chain; and detecting the labeled proteoglycan. 1. A method for assaying endoglycosidase activity , the method comprising:providing a proteoglycan having a glycosaminoglycan chain with a non-reducing end;treating the proteoglycan with a glycosyltransferase to incorporate a carbohydrate into the non-reducing end of the glycosaminoglycan chain, wherein the carbohydrate includes a click chemistry moiety;adding a label to the proteoglycan, wherein the label includes a click chemistry moiety that reacts to the click chemistry moiety of the carbohydrate such that the label attaches to the carbohydrate to form a labeled proteoglycan;immobilizing the labeled proteoglycan on a multi-well plate, wherein the multi-well plate includes a specific anti-proteoglycan antibody for binding the labeled proteoglycan;treating the labeled proteoglycan with an endoglycosidase specific to the glycosaminoglycan chain; anddetecting the labeled proteoglycan.2. The method of claim 1 , wherein the proteoglycan is a recombinant proteoglycan claim 1 , the glycosyltransferase is a recombinant glycosyltransferase claim 1 , and the endoglycosidase is a recombinant ...

GNE AS A THERAPEUTIC AGENT

The invention relates to composition and methods for expressing UDP-GlcNAc 2-Epimerase/ManNAc Kinase enzyme (GNE) in a living organism. In preferred embodiments, the invention relates to treating disease condition that involves use of therapeutically effective amount of a composition described herein. 1. A method of treating a subject , comprising administration to the subject a composition comprising AAV vector comprising at least a DNA molecule encoding GNE or a therapeutic fragment thereof , wherein the vector capsid comprises amino acid sequence of SEQ ID 18 or SEQ ID 19.2. A method of treating a subject , comprising administering to the subject a composition comprising a gene therapy vector , which comprises at least a DNA molecule backbone of SEQ ID 1 or 2 , wherein the human gene insert encodes for GNE or a therapeutic fragment thereof3. A composition comprising DNA molecule described by SEQ ID 1 or 2.4. A method of or , wherein the composition has a net negative charge.5. A composition of claim 3 , wherein the composition has a net negative charge6. A method of or claim 3 , wherein the composition is administered intravenously.7. A composition as claimed in claim 3 , wherein the composition is a gene therapy vector.8. A method as claimed in or claim 3 , wherein GNE has at least one mutation within the allosteric domain.9. A method as claimed in or claim 3 , wherein the composition further comprises at least one eukaryotic enhancer.10. A method as claimed in or claim 3 , wherein subsequent to the administration of the composition claim 3 , the subject experiences an increase in sialic content.11. A method as claimed in or claim 3 , wherein the subject has at least one mutation in the gene encoding GNE.12. A method as claimed in or claim 3 , comprising administering the composition to a limb or limbs of the subject.13. A method of as claimed in or claim 3 , wherein subsequent to the administration of the composition claim 3 , the subject experiences an ...

Destroying Cancer Cells While Maintaining Healthy Cell Integrity

The present invention teaches a system and method for identifying, targeting and destroying cancer cells without harming healthy tissue. This invention uses a vector engineered virus to selectively seek out cells that are both hotter than normal with a pH factor that is lower than normal thereby identifying cells that are cancerous regardless of location. Cancer succeeds for two reasons: i) rapid growth and ii) failure of the body's immune system to recognize the aberrant cells. This novel approach of using a dual vectored virus creates a dominant preference for locating and attaching to cancer cells, eliminating the need for chemotherapy, radiation therapy, and most major surgeries.

Polypeptides Having Alpha-Glucuronidase Activity And Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having alpha-glucuronidase activity, catalytic domains and polynucleotides encoding the polypeptides, catalytic domains. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides or catalytic domains. 1. An isolated polypeptide having alpha-glucuronidase activity , selected from the group consisting of:(a) a polypeptide having at least 80% sequence identity to the mature polypeptide of SEQ ID NO:2; orat least 95%, sequence identity to the mature polypeptide of SEQ ID NO:4 orat least 95%, sequence identity to the mature polypeptide of SEQ ID NO:6 orat least 60% sequence identity to the mature polypeptide of SEQ ID NO:8;(b) a polypeptide encoded by a polynucleotide that hybridizes under high stringency conditions with (i) the mature polypeptide coding sequence of SEQ ID NO:1, (ii) the cDNA sequence thereof, or (iii) the full-length complement of (i) or (ii); oror under very high stringency conditions with (iv) the mature polypeptide coding sequence of SEQ ID NO:3, (v) the cDNA sequence thereof, or (vi) the full-length complement of (iv) or (v);or under very high stringency conditions with (vii) the mature polypeptide coding sequence of SEQ ID NO:5, (viii) the cDNA sequence thereof, or (ix) the full-length complement of (vii) or (viii);or under medium stringency conditions with (x) the mature polypeptide coding sequence of SEQ ID NO:7, (xi) the cDNA sequence thereof, or (xii) the full-length complement of (x) or (xi);(c) a polypeptide encoded by a polynucleotide having at least 80% sequence identity to the mature polypeptide coding sequence of SEQ ID NO:1 or the cDNA sequence thereof or having at least 90% sequence identity to the mature polypeptide coding sequence of SEQ ID NO:3 or the cDNA sequence thereof orhaving at least 85% sequence identity to the mature polypeptide coding sequence of SEQ ID NO:5 or ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND A MUSHROOM EXTRACT OR POWDER

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and a mushroom (preferably maitake, shiitake, or reishi mushroom) extract or powder. The invention also relates to the combination of sulforaphane or a derivative thereof and a mushroom (preferably maitake, shiitake, or reishi mushroom) extract or powder. The present invention also relates to the combination of a broccoli extract or powder and a mushroom (preferably maitake, shiitake, or reishi mushroom) extract or powder. The present provides compositions and methods relating to these combinations. 1. An orally administrable composition comprising:a sulforaphane precursor;an enzyme capable of converting the sulforaphane precursor to sulforaphane;an enzyme potentiator; anda mushroom extract or powder.2. The orally administrable composition of claim 1 , wherein the sulforaphane precursor comprises glucoraphanin.3. The orally administrable composition of claim 1 , wherein the enzyme capable of converting the sulforaphane precursor to sulforaphane comprises myrosinase.4. The orally administrable composition of claim 1 , wherein the enzyme potentiator comprises ascorbic acid.5. The orally administrable composition of claim 1 , wherein the composition comprises an enteric-coated dosage form.6. The orally administrable composition of claim 1 , wherein the mushroom extract or powder comprises maitake mushroom extract.7. The orally administrable composition of claim 1 , wherein the mushroom extract or powder comprises shiitake mushroom extract.8. The orally administrable composition of claim 1 , wherein the mushroom extract or powder comprises a mixture of maitake mushroom extract and shiitake mushroom extract.9. The orally administrable composition of claim 1 , wherein composition further comprises one or more additional components is selected from the group consisting of: quercetin claim 1 , an aminosugar ...

Compositions comprising sulforaphane or a sulforaphane precursor and a mushroom extract or powder

The present disclosure relates to the synergistic combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, a cofactor of the enzyme, and a glucan. The present disclosure also relates to the synergistic combination of sulforaphane or a derivative thereof and a glucan. The present disclosure also relates to the synergistic combination of a broccoli extract or powder and a glucan. The glucan may be a β-glucan. The glucan may be provided in a mushroom extract or powder selected from one or more of a maitake, a shiitake, or a reishi mushroom. Compositions and methods relating to these combinations are described.

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND URSOLIC ACID

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and ursolic acid, a salt, ester, amide, or derivative thereof. The invention also relates to the combination of a sulforaphane or a derivative thereof and ursolic acid, a salt, ester, amide, or derivative thereof. The invention also relates to the combination of a broccoli extract or powder and ursolic acid, a salt, ester, amide, or derivative thereof. The invention provides compositions and methods relating to these combinations. 1. An orally administrable composition comprising:a sulforaphane precursor;an enzyme capable of converting the sulforaphane precursor to sulforaphane;an enzyme potentiator; andursolic acid, a salt, ester, amide or a derivative thereof.2. The orally administrable composition of claim 1 , wherein the sulforaphane precursor comprises glucoraphanin.3. The orally administrable composition of claim 1 , wherein the enzyme capable of converting the sulforaphane precursor to sulforaphane comprises myrosinase.4. The orally administrable composition of claim 1 , wherein the enzyme potentiator comprises ascorbic acid.5. The orally administrable composition of claim 1 , wherein the composition comprises an enteric-coated dosage form.6. The orally administrable composition of claim 1 , further comprising one or more additional components selected from the group consisting of: quercetin claim 1 , an aminosugar claim 1 , a glycosaminoglycan claim 1 , avocado/soybean unsaponifiable claim 1 , a vitamin claim 1 , coffee fruit claim 1 , magnesium claim 1 , silymarin claim 1 , proanthocyanidins claim 1 , alpha- and beta-glucans claim 1 , curcumin claim 1 , phytosterols claim 1 , and phytostanols.7. The orally administrable composition of claim 1 , comprising glucoraphanin claim 1 , myrosinase claim 1 , ascorbic acid claim 1 , and ursolic acid.8. The orally administrable composition of claim 1 , ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND A MILK THISTLE EXTRACT OR POWDER

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and a milk thistle extract or powder. The invention also relates to the combination of a sulforaphane or a derivative thereof and a milk thistle extract or powder. The invention also relates to the combination of a broccoli extract or powder and a milk thistle extract or powder. The invention provides compositions and methods relating to these combinations. 1. An orally administrable composition comprising:a sulforaphane precursor;an enzyme capable of converting the sulforaphane precursor to sulforaphane;an enzyme potentiator; anda milk thistle extract or powder.2. The orally administrable composition of claim 1 , wherein the sulforaphane precursor comprises glucoraphanin.3. The orally administrable composition of claim 1 , wherein the enzyme capable of converting the sulforaphane precursor to sulforaphane comprises myrosinase.4. The orally administrable composition of claim 1 , wherein the enzyme potentiator comprises ascorbic acid.5. The orally administrable composition of claim 1 , wherein the composition comprises an enteric-coated dosage form.6. The orally administrable composition of claim 1 , further comprising one or more additional components selected from the group consisting of: quercetin claim 1 , an aminosugar claim 1 , a glycosaminoglycan claim 1 , avocado/soybean unsaponifiable claim 1 , a vitamin claim 1 , coffee fruit claim 1 , magnesium claim 1 , silymarin claim 1 , proanthocyanidins claim 1 , ursolic acid claim 1 , curcumin claim 1 , phytosterols claim 1 , and phytostanols.7. The orally administrable composition of claim 1 , comprising glucoraphanin claim 1 , myrosinase claim 1 , ascorbic acid claim 1 , and milk thistle extract.8. The orally adminsitrable composition of claim 1 , wherein the composition comprises broccoli extract or powder.9. A method of treating claim 1 , ...

AMYLASE WITH MALTOGENIC PROPERTIES

The present teachings provide an amylase with maltogenic properties. Nucleic acids encoding the maltogenic amylase and variants thereof, expression vectors, formulations, and host cells are also provided. Additional embodiments of the present teachings provide various methods of use and methods of manufacturing. 1. An isolated nucleic acid comprising the nucleotide sequence of SEQ ID NO: 1 or of a degenerate variant of SEQ ID NO: 1.2. An isolated nucleic acid comprising a sequence that encodes a polypeptide consisting of the amino acid sequence of SEQ ID NO: 3.3. An isolated nucleic acid comprising a sequence that hybridizes under stringent conditions to a hybridization probe the nucleotide sequence of which consists of SEQ ID NO: 1 , or the complement of SEQ ID NO: 1.4. An isolated nucleic acid comprising a sequence at least 66% , 67% , 68% , 69% , 70% , 75% , 80% , 85% , 90% , 95% , 98% , 99% , or 99.5% identical to SEQ ID NO: 1.5. The isolated nucleic acid of wherein the nucleic acid encodes a polypeptide that has starch hydrolysis activity.6. An isolated nucleic acid comprising a sequence that encodes a polypeptide at least 66% claim 4 , 67% claim 4 , 68% claim 4 , 69% claim 4 , 70% claim 4 , 75% claim 4 , 80% claim 4 , 85% claim 4 , 90% claim 4 , 95% claim 4 , 98% claim 4 , 99% claim 4 , or 99.5% identical to SEQ ID NO: 3 claim 4 , wherein the polypeptide has starch hydrolysis activity.7. An isolated nucleic acid comprising a sequence that encodes a polypeptide comprising the sequence of SEQ ID NO: 3 claim 4 , or SEQ ID NO: 3 with up to 50 conservative amino acid substitutions claim 4 , wherein the polypeptide has starch hydrolysis activity.8. A purified polypeptide claim 4 , the amino acid sequence of which comprises a sequence at least 66% claim 4 , 67% claim 4 , 68% claim 4 , 69% claim 4 , 70% claim 4 , 75% claim 4 , 80% claim 4 , 85% claim 4 , 90% claim 4 , 95% claim 4 , 98% claim 4 , 99% claim 4 , or 99.5% identical to SEQ ID NO: 3.9. A purified ...

Compositions and Methods for Modulating Growth of a Genetically Modified Gut Bacterial Cell

Compositions and methods are provided for modulating growth of a genetically modified bacterial cell present in a human organ, for modulating growth of a genetically modified bacterial cell in an organ (e.g., gut), for displacing at least a portion of a population of bacterial cells in an organ, and for facilitating gut colonization by a genetically modified bacterial cell. Also provided are genetically modified bacterial cells, e.g., cells that include a heterologous carbohydrate-utilization gene or gene set that provides for the ability to utilize as a carbon source a rare carbohydrate of interest that is utilized as a carbon source by less than 50% of bacterial cells present in a human microbiome. 1Bacteroides. A method of colonizing the gut of a subject with a genetically modified , non-naturally occurring cell , the method comprising administering to the subject both:{'i': Bacteroides', 'Bacteroides', 'Bacteroides, 'a) the genetically modified cell, wherein the genetically modified cell comprises a heterologous carbohydrate-utilization gene set that provides the genetically modified cell with an ability to utilize as a carbon source a porphyran and comprises at least twelve genes and one or more nucleic acids encoding a porphyranase; and'}b) porphyran.2B. plebeiusB. ovatus. The method of claim 1 , wherein the carbohydrate-utilization gene set comprises one or more nucleic acids encoding a porphyranase from the or genome.3. The method of claim 1 , wherein one of the nucleic acids encodes a protein having 80% or more sequence identity to SEQ ID NO: 19.4. The method of claim 1 , wherein one of the nucleic acids encodes a protein having 80% or more sequence identity to SEQ ID NO: 21.5. The method of claim 1 , wherein the carbohydrate-utilization gene set comprises one or more nucleic acids each selected from the group consisting of nucleic acids encoding a protein having 80% or more sequence identity to SEQ ID NOs: 14-34.6. The method claim 1 , wherein the ...

GENE TARGETS FOR IMPROVED ENZYME PRODUCTION IN FUNGI

Fungi that are genetically inactivated for the mstC gene (or a homolog thereof) are provided, which can also be genetically modified to increase production of heterologous proteins from a glucoamylase promoter. Methods of using these fungi, for example to degrade a biomass, are also provided. 1. An isolated fungus comprising a genetic inactivation of a mstC gene or homolog thereof.2. The isolated fungus of claim 1 , wherein the isolated fungus is in class Eurotiomycetes or Sordariomycetes.3. The isolated fungus of claim 1 , wherein the mstC gene or homolog thereof is genetically inactivated by nonsynonymous mutation or by insertional mutation.4. The isolated fungus of claim 1 , wherein the mstC gene genetically inactivated comprises a nucleic acid molecule comprising at least 95% claim 1 , at least 98% claim 1 , at least 99% claim 1 , or 100% sequence identity to SEQ ID NO: 1 claim 1 , 3 claim 1 , or nt 82 to 1764 of SEQ ID NO: 1 claim 1 , or wherein the mstC homolog is a NCU01633 gene comprising at least 95% claim 1 , at least 98% claim 1 , at least 99% claim 1 , or 100% sequence identity to SEQ ID NO: 9 claim 1 , 10 claim 1 , or nt 652 to 2250 of SEQ ID NO: 10.5. The isolated fungus of claim 1 , wherein the mstC gene genetically inactivated encodes a protein comprising at least 95% claim 1 , at least 98% claim 1 , at least 99% claim 1 , or 100% amino acid sequence identity to SEQ ID NO: 2 claim 1 , or wherein the mstC homolog genetically inactivated encodes a NCU01633 protein is a gene comprising at least 95% claim 1 , at least 98% claim 1 , at least 99% claim 1 , or 100% amino acid sequence identity to SEQ ID NO: 11.6. The isolated fungus of claim 1 , further comprising a glucoamylase promoter operably linked to a heterologous protein coding sequence.7. The isolated fungus of claim 6 , wherein the isolated fungus produces a heterologous protein.8. The isolated fungus of claim 7 , wherein the heterologous protein is a heterologous enzyme claim 7 , or a chimeric ...

METHODS AND COMPOSITIONS FOR THE DISRUPTION OF BIOFILMS AND TREATMENT OF DISORDERS CHARACTERIZED BY THE PRESENCE OF BIOFILMS

Methods and compositions are provided for the disruption of biofilms and the treatment of disorders characterized by the presence of biofilms and/or abnormally viscous and/or cohesive bodily secretions, such as mucus and sputum. Disorders that can be effectively treated using the disclosed compositions and methods include cystic fibrosis (CF), endocarditis, urinary tract infections, middle-ear infections, chronic sinusitis, gingivitis, periodontal disease, bronchiectasis, chronic obstructive pulmonary disease (COPD), asthma, bronchitis, neonatal meconium aspiration syndrome, smokers' cough, chronic tonsillitis, chronic vaginitis, and fungal or bacterial infections. The compositions, which contain an effective amount of trisodium citrate and ammonium chloride, may be administered alone or in combination with one or more known therapeutic agents. 131-. (canceled)32. A method for treating or preventing a disorder characterized by the presence of biofilm in a subject in need thereof , the method comprising administering to the subject a composition comprising trisodium citrate and ammonium chloride in an amount effective to disrupt the biofilm compared to prior to administration , wherein the disorder is selected from the group consisting of: cystic fibrosis (CF) , endocarditis , urinary tract infections , middle-ear infections , chronic sinusitis , chronic tonsillitis , gingivitis , periodontal disease , bronchiectasis , chronic obstructive pulmonary disease (COPD) , asthma , neonatal meconium aspiration syndrome , smokers' cough , chronic tonsillitis , chronic vaginitis , and infections of implanted devices , such as catheters , heart valves , intrauterine devices and joint prostheses.33. A method for treating or preventing a disorder characterized by the presence of biofilm in a subject in need thereof , the method comprising administering to the subject a composition comprising trisodium citrate and ammonium chloride in an amount effective to disrupt the biofilm ...

ENZYME COMPOSITION FOR THERAPEUTIC MANAGEMENT OF MUSCLE SORENESS

The present invention discloses a combination of digestive enzymes (Protease, Amylase, Lactase, Lipase, Cellulase)—DigeZyme® for the therapeutic management of delayed onset muscle soreness (DOMS) 1. A method for therapeutic management of delayed onset muscle soreness using a comprehensive digestive enzyme blend comprising Protease , Amylase , Lactase , Lipase and Cellulase (DigeZyme®) , said method comprising steps of administering effective concentrations of the enzyme blend to mammals presenting with symptoms of delayed onset muscle soreness.2. The method as in claim 1 , wherein the individual enzymes in the digestive blend are present in the concentrations:a) amylase: 24000 DU/g, b) Cellulase: 1100 CU/g, c) Lipase: 200 FIP/g, d) Lactase: 4000 ALU/g and e) Protease: 6000 PC/g.3. The method as in claim 1 , wherein the symptoms of delayed onset muscle soreness include pain claim 1 , tenderness claim 1 , inflammation claim 1 , muscle damage and flexibility.4. The method as in claim 1 , wherein the mammal is human.5. A composition comprising a comprehensive digestive enzyme blend of Protease claim 1 , Amylase claim 1 , Lactase claim 1 , Lipase and Cellulase (DigeZyme®) for use in therapeutic management of Delayed Onset Muscle Soreness (DOMS).6. The composition as in claim 2 , wherein the individual enzymes in the digestive blend are present in the concentrations:a) amylase: 24000 DU/g, b) Cellulase: 1100 CU/g, c) Lipase: 200 FIP/g, d) Lactase: 4000 ALU/g and e) Protease: 6000 PC/g. The invention in general relates to enzymes. More specifically the invention relates to use of the digestive enzymes for the alleviating the symptoms of delayed on set muscle soreness (DOMS).Delayed on set muscle soreness (DOMS) is an exercise induced phenomenon and is a recurrent form of sports injury. It is presented as a sensation of discomfort, predominantly with the skeletal muscles following unaccustomed physical activity. Associated symptoms include muscle shortening, increased ...

Enzyme Formulation for Reducing Histamine Intolerance

Disclosed is a formulation of the following enzymes: Alpha-galactosidase, Alpha amylase, Beta Glucanase, Lactase, BioCor DPP=IV (Proprietary blend) and Pectinase, which has been found to be effective in treating histamine intolerant people, and causing a significant improvement in a wide variety of pathologies and symptoms, including, but not limited to: inflammation, pruritus, urticaria, hypotension, tachycardia, fatigue, migraines, conjunctivitis, incontinence, nasal congestion, panic attacks, acid reflux, depression and angioedema. 1. A method of treating , preventing or ameliorating histamine intolerance , the method comprising administering a subject a formulation comprising Alpha-galactosidase , Alpha amylase , Beta Glucanase , Lactase , BioCor DPP-IV and Pectinase.2. The method of wherein the active ingredients in the formulation have the following dosages: Alpha-galactosidase: 80 GaLU; Alpha amylase claim 1 , 150 DU; Beta Glucanase claim 1 , 70 BGU; Lactase claim 1 , 1 claim 1 ,000 ALU; BioCor DPP-IV claim 1 , 80 mg claim 1 , and Pectinase: 17 ENDO-PGU.3. The method of wherein the active ingredients are administered to the subject at twice the dosages therein with each meal consumed.4. The method of wherein the formulation is encapsulated in a vegetable capsule comprising cellulose and distilled water.5. The method of wherein the formulation does not contain any of the following: milk/casein claim 4 , gluten claim 4 , dairy claim 4 , egg claim 4 , soy claim 4 , corn claim 4 , peanuts claim 4 , tree nuts claim 4 , fish and shellfish claim 4 , and claim 4 , artificial colors claim 4 , flavors or preservatives.6. A method of treating claim 4 , preventing or ameliorating urticaria or depression associated with histamine intolerance claim 4 , the method comprising administering a subject a formulation comprising:Alpha-galactosidase, Alpha amylase, Beta Glucanase, Lactase, BioCor DPP-IV and Pectinase.7. The method of wherein the active ingredients in the ...

Xylosidase having improved enzymatic activity

A xylosidase having improved enzymatic activity is disclosed. The amino acid sequence of the xylosidase is a modified amino acid sequence of SEQ ID NO: 2, wherein the modification is a substitution of phenylalanine at position 35 with glutamate, and/or a substitution of glutamine at position 41 with histidine.

Xylanase Variants and Polynucleotides Encoding Same

The present invention relates to xylanase variants, polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; compositions comprising the xylanase variants and methods of using the variants. 1. A method for obtaining a xylanase variant , comprising(a) introducing into a parent xylanase a substitution at one or more positions corresponding to positions 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 18, 19, 31, 32, 33, 34, 39, 43, 44, 45, 46, 48, 50, 58, 59, 61, 62, 64, 65, 67, 68, 79, 82, 88, 90, 94, 101, 102, 104, 110, 112, 113, 116, 119, 120, 123, 126, 127, 128, 129, 131, 135, 143, 145, 146, 159, 160, 165, 168, 176, 179, 181, 188, 191, 194, 195, 196, 197, 205, 209, 212, 217, 218, 221, 224, 231, 235, 237, 238, 242, 269, 280, 282, 295, 298, 299, 300, 302, 305, 306, 307, 311, 312, 313, 322, 323, 324, 333, 334, 335, 336, 337, 338, 339, 340, 342, 343, 344, 345, 346, 347, 349, 350, 354, 357, 359, 360, 363, 364, 366, 367, 368, 371, 373, 374, 376, 377, 378, 380, 385, 388, 390 and 391 of SEQ ID NO: 1, wherein the xylanase variant has xylanase activity and has at least 70%, e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to SEQ ID NO: 1; and(b) recovering the xylanase variant.2. The method of claim 1 , wherein the xylanase variant has improved thermostability relative to the parent.3. The method of claim 1 , wherein the parent xylanase has at least 70% claim 1 , e.g. claim 1 , at [[at]] least 75% claim 1 , at least 80% claim 1 , at least 85% claim 1 , at least 90% claim 1 , at least 95% claim 1 , at least 96% claim 1 , at least 97% claim 1 , at least 98% claim 1 , at least 99% or 100% sequence identity to SEQ ID NO: 1.4. The method of claim 1 , wherein the one or more substitutions is selected from the group consisting of A2D claim 1 , A2Q claim 1 , A2G claim 1 , A2W claim 1 , A2P claim 1 , A2L claim 1 , A2Y ...

Ready to eat cold beverage cakes with ingredients

Cold and ready to eat beverage cakes, and with a variety of ingredient combinations are suitable for healthy consumption. The beverage cakes are soft in texture and high in nutrition. People can save the time and energy of preparing and cooking of the food. Serving size can be a single serving, and a six pack of servings. Beverage cakes are also created as beverage egg cakes, beverage plus salt source cakes, beverage seafood cakes, beverage meat cakes, beverage bubbles, beverage balls, beverage patties, and beverage sausages. They can be served as cold and hot food for breakfast, lunch, snack, and dinner. They can also be used as animal food, baby food, for children with less teeth, for elderly people, and for sick people. Cold and ready to eat beverage cakes with ingredients offer the consumers an easy and convenient way to obtain an affordable, nutritious, and delicious meal.

VARIANT MALTOGENIC ALPHA-AMYLASE

The present invention relates to a variant polypeptide having maltogenic alpha-amylase activity wherein the polypeptide comprises an amino acid sequence, which, when aligned with an amino acid sequence of SEQ ID NO: 1, comprises an amino acid substitution F188L/I, S200N, and D261G, and optionally a further amino acid substitution T288P, wherein the amino acid substitutions are determined with reference to SEQ ID NO: 1, and wherein the polypeptide has an amino acid sequence which has at least 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or at least 99% identity to the amino acid sequence of SEQ ID NO: 1. The invention also relates to a process for the preparation of a dough or a baked product wherein the variant polypeptide is used. 1. A variant polypeptide having maltogenic alpha-amylase activity wherein the polypeptide comprises an amino acid sequence , which , when aligned with an amino acid sequence of SEQ ID NO: 1 , comprises an amino acid substitution F188L/I , 5200N , and D261G , and optionally a further amino acid substitution T288P , wherein the amino acid substitutions are determined with reference to SEQ ID NO: 1 , and wherein the polypeptide has an amino acid sequence which has at least 70% , 75% , 80% , 85% , 90% , 95% , 96% , 97% , 98% , or at least 99% identity to the amino acid sequence of SEQ ID NO: 1.2. The polypeptide according to claim 1 , wherein the polypeptide has a decreased dependency on calcium ions for thermostability as compared to a reference polypeptide not having the amino acid substitutions F188L/I claim 1 , 5200N claim 1 , and D261G claim 1 , and optionally a further amino acid substitution T288P.3. A polypeptide having maltogenic alpha-amylase activity claim 1 , optionally according to claim 1 , wherein the polypeptide has at least 40% residual maltogenic alpha-amylase activity after incubating the polypeptide in 50 mM malic acid buffer pH 5.2 claim 1 , containing 50 mM NaCl and 0.05% BSA and 2 mM EDTA at a temperature of 87.4° C. ...

Waxy Maize Starches and Methods of Making and Using Them

The present disclosure relates to waxy maize starches having desirably high process stability, and to methods relating to them, including methods for making and using them. One aspect of the disclosure is a waxy maize starch having an amyiopectin content in the range of 90-100%; wherein the amyiopectin fraction of the waxy maize starch has at least 28.0% DP3-12 branches: and no more than 53.0% DP 13-24 branches, no more than 16.0% DP 25-36 branches. Such waxy maize starches can be advantaged over conventional waxy maize starches in that they can have increased process stability, especially with respect to freeze-thaw stability. Methods of making the starch materials, using exo-hydrolyzing enzymes and methods of using the starch materials in food products are also described. 1. A waxy maize starch having an amylopectin content in the range of 90-100% , whereinthe amylopectin fraction of the waxy maize starch has no more than 53.0% DP13-24 branches or', 'a DP3-12 value that is at least 3.0 percentage points greater than the DP3-12 value for native waxy maize starch; and', 'a DP13-24 value that is at least 3.0 percentage points less than the DP13-24 value for native waxy maize starch., 'at least 26.0% DP3-12 branches; and'}2. The waxy maize starch according to claim 1 , wherein the amylopectin fraction of the waxy maize starch has in the range of 27.5-47.5% DP3-12 branches.3. The waxy maize starch according to claim 1 , wherein the amylopectin fraction of the waxy maize starch has at in the range of 32.0-50.0% DP3-12 branches.4. The waxy maize starch according to claim 1 , wherein the amylopectin fraction of the waxy maize starch has at least 24.0% DP6-12 branches.5. The waxy maize starch according to claim 1 , wherein the amylopectin fraction of the waxy maize starch has in the range of 25.0-32.0% DP6-12 branches.6. The waxy maize starch according to claim 1 , wherein the amylopectin fraction of the waxy maize starch has in the range of 3.0-25.0% DP3-5 branches.7. The ...

DELIVERING ENZYME USING AN INJECTABLE HYDROGEL DEPOT

Compositions and methods for delivering enzymes in enzyme hydrogel formulations are disclosed. More particularly, the present disclosure relates to injectable enzyme hydrogel formulations and delivery of injectable enzyme hydrogel formulations. Also disclosed are methods for GALNS enzyme replacement therapy and lysosomal enzyme replacement therapy. 1. A delivery system for delivering an enzyme hydrogel formulation comprising: an applicator and an enzyme hydrogel formulation , the enzyme hydrogel comprising an enzyme , a polymer , and a buffer solution.2. The delivery system of claim 1 , wherein the enzyme comprises a recombinant enzyme.3. The delivery system of claim 1 , wherein the enzyme comprises a human enzyme.4. The method of claim 1 , wherein the enzyme is N-acetylgalactosamine 6-sulfate sulfatase (GALNS).5. The method of claim 1 , wherein the enzyme is a lysosomal enzyme selected from the group consisting of α-L-iduronidase claim 1 , Iduronate-2-sulfate sulfatase claim 1 , Heparan N sulfatase claim 1 , α-N-acetylglucosaminidase claim 1 , acetyl-CoA: α-glucosaminide acetyltransferase claim 1 , N-acetylglucosamine 6-sulfatase claim 1 , β-galactosidase claim 1 , Arylsulfatase B claim 1 , β-Glucuronidase claim 1 , Hyaluronidase claim 1 , acid α-glucosidase claim 1 , glucocerebrosidase claim 1 , and combinations thereof.6. The delivery system of claim 1 , wherein the polymer comprises polyethylene glycol (PEG) claim 1 , polyethylene glycol acrylate (PEGAc) claim 1 , poly(glycolic acid) (PGA) claim 1 , poly(L-lactic acid) (PLA) claim 1 , poly(lactide-co-glycolide) (PLGA) claim 1 , poly(L-lactide) (PLLA) claim 1 , poly(D claim 1 ,L-lactide) (p(DLLA)) claim 1 , poly(ethylene glycol)1-co-poly(L-lactide) (PEG-PLLA) claim 1 , poly(ε-caprolactone (PCL) claim 1 , poly(L-lactide-co-ε-caprolactone) (P(LLA-CL)) claim 1 , poly(ε-caprolactone-co-ethyl ethylene phosphate (P(CL-EEP)) claim 1 , poly(ethylene-co-vinyl alcohol) claim 1 , poly(ethylenimine) claim 1 , ...

METHODS AND COMPOSITIONS FOR IMPROVING ENGINEERED MICROBES

The present disclosure provides a bacterial composition, comprising: at least one genetically engineered bacterial strain that fixes atmospheric nitrogen in an agricultural system, wherein the bacterial strain comprises a modification in or one or more genes selected from the group consisting of bcsll, bcslll, yjbE, fhaB, pehA, glgA, otsB, treZ, and cysZ. The present disclosure further provides a bacterial composition and method for increasing the colonization of a plant growth promoting bacterial strain on a plant, wherein the plant growth promoting bacterial strain has been remodeled to increase colonization of said plant, In a further aspect, the present disclosure provides methods of increasing nitrogen or nitrogen fixation available to a plant. 1. (canceled)2. A bacterial composition , comprising:a bacterial strain, wherein said strain has been remodeled to increase colonization of said bacterial strain on a plant.3. The bacterial composition of claim 2 , wherein said colonization of said bacterial strain occurs on a root of said plant.4. The bacterial composition of claim 2 , wherein said bacterial strain comprises a genetic modification in an enzyme or pathway involved in production of exopolysaccharides.50. The bacterial composition of claim claim 2 , wherein said genetic modification is in a gene selected from the group consisting of bcsII claim 2 , bcsIII claim 2 , and yjbE.6. The bacterial composition of claim 2 , wherein said bacterial strain comprises a genetic modification in an enzyme or pathway involved in production of a filamentous hemagglutinin.70. The bacterial composition of claim claim 2 , wherein said genetic modification is in a fhaB gene.8. The bacterial composition of claim 2 , wherein said bacterial strain comprises a genetic modification in an enzyme or pathway involved in production of an endo-polygalaturonase.90. The bacterial composition of claim claim 2 , wherein said genetic modification is in a pehA gene.10. The bacterial ...

Polypeptides

The invention relates to polypeptides having hydrolytic activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. A cleaning composition comprising:(a) at least 0.01 ppm GH114 glycosyl hydrolase enzyme having alpha-1,4-polygalactosaminidase activity, wherein the GH114 glycosyl comprises one or both motif(s) [VLI]XE[EDSQ]C (SEQ ID NO 60) or CY[FLIV][SDN][ATVG] (SEQ ID NO 61); and(b) an anionic surfactant selected from the group consisting of sulfates and solfonates.2. The cleaning composition according to claim 1 , further comprising at least one nonionic surfactant.3. The cleaning composition according to claim 1 , wherein the GH114 glycosyl hydrolase comprises one or both motifs DYQ[L]G (SEQ ID NO 62) or FQ[TAV]Q[PSD] (SEQ ID NO 63).4. The cleaning composition according to claim 3 , wherein the glycosyl hydrolase comprises one or both motifs AEECG (SEQ ID NO 64) or NAFQ[AT]Q (SEQ ID NO 65).5. The cleaning composition according to claim 1 , wherein the GH114 glycosyl hydrolase comprises one or both motifs GXXVX[NHQTS]IEY[PG] (SEQ ID NO 68) claim 1 , VICYF (SEQ ID NO 69)6. The cleaning composition according to claim 5 , wherein the GH114 glycosyl hydrolase comprises the motif ICYFSA (SEQ ID NO 70)7. The cleaning composition according to claim 5 , wherein the GH114 glycosyl hydrolase comprises the motif DFAVL (SEQ ID NO 71)8. The cleaning composition according to claim 1 , wherein the GH114 glycosyl hydrolase comprises one or both motifs WQWQL (SEQ ID NO 66) or [VLI][GASD]LKN[DGS][VLIP] (SEQ ID NO 67).9. The cleaning composition according to claim 3 , wherein the GH114 glycosyl hydrolase is selected from the group consisting of: a polypeptide having at least 80% sequence identity to the polypeptide of SEQ ID NO 3 claim 3 , SEQ ID NO 6 claim 3 , SEQ ID NO 9 claim 3 , SEQ ID NO 12 claim 3 , SEQ ID NO ...

ENZYMATIC REMOVAL OF STERYL GLYCOSIDES

The present invention provides compositions and methods related to the production and use of enzymes suitable for reducing the amount of steryl glycosides or saturated monoacyl glycerols in a lipid mixture. 1. A method for reducing steryl glycoside in a sample , comprising:In a reaction mixture, mixing a thermostable enzyme with a sample comprising steryl glycoside under a condition suitable for said thermostable enzyme for a suitable period of time to degrade said steryl glycoside, thereby reducing steryl glycoside in said sample to obtain a processed sample.2. The method of claim 1 , wherein said sample comprises oil claim 1 , fat claim 1 , or biofuel.3. The method of claim 2 , wherein said biofuel comprises biodiesel.4. The method of claim 1 , wherein said steryl glycoside comprises steryl glucoside.5. The method of claim 1 , wherein said steryl glycoside has a solubility that is more than 50 ppm.6. The method of claim 1 , wherein said steryl glycoside has a solubility that is more than 80 ppm.7. The method of claim 1 , wherein said steryl glycoside has a solubility that is more than 100 ppm.8. The method of claim 1 , wherein said thermostable enzyme is capable of hydrolyzing the glycosidic bond of a steryl glucoside or acylated steryl glucoside.9. The method of claim 1 , wherein said thermostable enzyme comprises a glycosidase enzyme.10. The method of claim 1 , wherein said thermostable enzyme comprises a glucosidase enzyme.11. The method of claim 1 , wherein said thermostable enzyme comprises a variant of an enzyme selected from Table 1.12. The method of claim 1 , wherein said thermostable enzyme comprises a variant having an amino acid sequence that has at least 95% identity to a sequence selected from the sequences of Table 1.13. The method of claim 1 , wherein said thermostable enzyme comprises an amino acid sequence selected from the sequences of Table 1.14. The method of claim 1 , wherein said sample comprises 0.1% to 30% of water.15. The method of claim 1 ...

PREPARATION COMPRISING ARABINOXYLO-OLIGOSACCHARIDES

The present invention related to an arabinoxylo-oligosaccharide composition comprising at least one arabinose unit linked to one of the xylose units of the backbone, per molecule, wherein the at least one arabinose unit is an α-L-arabinofuranosyl, wherein said composition has an xylo-oligosaccharide backbone with a degree of polymerization of 1-10. 1. An arabinoxylo-oligosaccharide composition comprising at least one arabinose unit linked to one of the xylose units of the backbone , per molecule , wherein the at least one arabinose unit is an α-L-arabinofuranosyl , wherein said composition has a xylo-oligosaccharide backbone with a degree of polymerization of 1-10 , wherein the composition comprise at most 10% monosaccharides and/or at most 10% xylooligosaccharides.2. The arabinoxylo-oligosaccharide composition according to claim 1 , wherein the arabinoxylo-oligosaccharide composition has an average degree of arabinose substitution of 0.2-0.7 preferably claim 1 , 0.3-0.6 claim 1 , preferably 0.35-0.50 claim 1 , preferably 0.4.3Bifidobacterium. The arabinoxylo-oligosaccharide composition according to claim 1 , wherein the arabinoxylo-oligosaccharide composition selectively is adapted to stimulate the growth of spp.4Bifidobacterium. The arabinoxylo-oligosaccharide composition according to claim 1 , wherein the spp belong to strains adapted to ferment arabinoxylo-oligosaccharides or the arabinose substituents on the oligosaccharides.5BifidobacteriumBifidobacterium adolescentis, Bifidobacterium longum, Bifidobacterium catenulatum, Bifidobacterium animalis, Bifidobacterium pseudolongum, Bifidobacterium gallicum, Bifidobacterium lactis, Bifidobacterium infantis, Bifidobacterium bifidum, Bifidobacterium angulatumBifidobacterium breve.. The arabinoxylo-oligosaccharide composition according to or claim 1 , wherein the spp is selected from the group consisting of or6Bifidobacterium. Synbiotic preparation comprising arabinoxylo-oligosaccharide composition according to claim 1 ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND A MUSHROOM EXTRACT OR POWDER

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and a mushroom (preferably maitake, shiitake, or reishi mushroom) extract or powder. The invention also relates to the combination of sulforaphane or a derivative thereof and a mushroom (preferably maitake, shiitake, or reishi mushroom) extract or powder. The present invention also relates to the combination of a broccoli extract or powder and a mushroom (preferably maitake, shiitake, or reishi mushroom) extract or powder. The present provides compositions and methods relating to these combinations. 121-. (canceled)22. An orally administrable composition comprising a broccoli extract or powder and a mushroom extract or powder.23. The orally administrable composition of claim 22 , wherein the broccoli extract or powder comprises glucoraphanin in an amount of about 1 to about 75% w/w.24. The orally administrable composition of claim 22 , wherein the broccoli extract or powder comprises myrosinase.25. The orally administrable composition of claim 22 , further comprising an enzyme potentiator.26. The orally administration composition of claim 22 , wherein the enzyme potentiator comprises ascorbic acid.27. The orally administrable composition of claim 22 , wherein the composition comprises an enteric dosage form.28. The orally administrable composition of claim 22 , wherein the mushroom extract or powder comprises one or more mushroom extracts or powders selected from the group of: maitake mushroom extract claim 22 , shiitake mushroom extract claim 22 , and reishi mushroom extract.29. The orally administrable composition of claim 22 , comprising a maitake mushroom extract comprising one or more glucans.30. The orally administrable composition of claim 22 , comprising a maitake mushroom extract comprising beta-glucan.31. The orally administrable composition of claim 22 , comprising a shiitake mushroom ...

Compositions comprising sulforaphane or a sulforaphane precursor and a mushroom extract or powder

The present disclosure relates to the synergistic combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, a cofactor of the enzyme, and a glucan. The present disclosure also relates to the synergistic combination of sulforaphane or a derivative thereof and a glucan. The present disclosure also relates to the synergistic combination of a broccoli extract or powder and a glucan. The glucan may be a β-glucan. The glucan may be provided in a mushroom extract or powder selected from one or more of a maitake, a shiitake, or a reishi mushroom. Compositions and methods relating to these combinations are described.

ENZYME COMPOSITION FOR SUGAR METABOLIC REGULATION

Disclosed is an enzyme composition for regulating sugar metabolism which can regulate the absorption of glucose into the body by converting the carbohydrates in food to a form of sugar that is not absorbed in the stomach and the like before being decomposed in the small intestine into glucose by the activity of various enzymes such as maltase, sucrase, or lactase and the like and absorbed, wherein the enzyme composition includes: one or more enzymes selected from the group consisting of glucoamylase, sucrase and lactase; glucose oxidase; and transglucosidase. 1. An enzyme composition for regulating sugar metabolism , comprising:one or more enzymes selected from the group consisting of glucoamylase, sucrase and lactase;glucose oxidase; andtransglucosidase.2. The composition of claim 1 , further comprising catalase.3. The composition of claim 2 , wherein all of glucoamylase claim 2 , sucrase claim 2 , lactase claim 2 , glucose oxidase claim 2 , transglucosidase and catalase are comprised.4. The composition of claim 3 , further comprising one or more types of amylases selected from α-amylase and β-amylase. The present invention relates to an enzyme composition for regulating sugar metabolism, and more particularly, to an enzyme composition for regulating sugar metabolism, which includes one or more enzymes selected from the group consisting of glucoamylase, sucrase and lactase; glucose oxidase; and transglucosidase.Saccharides are important substances constituting the living organism and used as an energy source, and particularly, glucose is very important as a pivotal compound of carbohydrate metabolism in the human body.While sugar is an essential compound necessary for the human body, excessive ingestion of glucose may cause obesity and a metabolic imbalance may lead to various diseases such as diabetes.A representative example of diseases caused by the imbalance of sugar metabolism is hyperglycemia. Hyperglycemia refers to a condition in which a blood sugar level ...

Structured Liquid Compositions

Microfibrillated cellulose, derived from vegetables or wood, can be used to provide a liquid composition which is compatible with a broad range of ingredients suitable for consumer applications, including enzymes, while still providing good structuring of the liquid composition, without affecting ease of pour. 1. A liquid composition comprising:a) surfactant, andb) microfibrillated cellulose derived from vegetables or wood.2. The composition according to claim 1 , wherein the surfactant is selected from the group consisting of: anionic surfactant claim 1 , nonionic surfactant claim 1 , cationic surfactant claim 1 , and mixtures thereof.3. The composition according to claim 1 , wherein the composition comprises from about 0.5% to about 40 wt % of the surfactant.4. The composition according to claim 1 , wherein the microfibrillated cellulose has an aspect ratio (l/d) of from about 50 to about 200 claim 1 ,000.5. The composition according to claim 1 , wherein the microfibrillated cellulose is derived from vegetables or wood claim 1 , wherein the vegetables or wood comprises less than about 10% soluble fibre as a percentage of total fibre.6. The composition according to claim 1 , wherein the microfibrillated cellulose is derived from sugar beet claim 1 , chicory root claim 1 , or mixtures thereof.7. The composition according to claim 1 , wherein the composition comprises from about 0.05 to about 10 wt % of the microfibrillated cellulose.8. The composition according to claim 1 , wherein the composition comprises sufficient microfibrillated cellulose to provide a yield stress of greater than about 0.005 Pa.9. The composition according to claim 1 , wherein the composition comprises enzymes selected from the group consisting of: cellulases claim 1 , endoglucanase with activity towards xyloglucan claim 1 , and mixtures thereof.10. The composition according to claim 1 , wherein the composition further comprises a suspended insoluble material.11. A liquid composition ...

Cellulolytic enzyme compositions and uses thereof

The present invention relates to recombinant filamentous fungal host cells producing cellulolytic enzyme compositions and methods of producing and using the compositions. 123-. (canceled)24Aspergillus fumigatusAspergillus fumigatusAspergillus fumigatusPenicillium. A recombinant filamentous fungal host cell , comprising polynucleotides encoding: (a) an cellobiohydrolase I; (b) an cellobiohydrolase II; (c) an beta-glucosidase or a variant thereof; and (d) a sp. GH61 polypeptide having cellulolytic enhancing activity; or homologs thereof;{'i': 'Aspergillus fumigatus', 'wherein the cellobiohydrolase I or homolog thereof is selected from the group consisting of(i) a cellobiohydrolase I comprising amino acids 27 to 532 of SEQ ID NO: 2;(ii) a cellobiohydrolase I comprising an amino acid sequence having at least 90% sequence identity to amino acids 27 to 532 of SEQ ID NO: 2;(iii) a cellobiohydrolase I encoded by a polynucleotide comprising a nucleotide sequence having at least 90% sequence identity to nucleotides 79 to 1596 of SEQ ID NO: 1; and(iv) a cellobiohydrolase I encoded by a polynucleotide that hybridizes under high stringency conditions with the full-length complement of nucleotides 79 to 1596 of SEQ ID NO: 1, wherein high stringency conditions are defined as prehybridization and hybridization at 42° C. in 5×SSPE, 0.3% SDS, 200 micrograms/ml sheared and denatured salmon sperm DNA, and 50% formamide, and washing three times each for 15 minutes using 2×SSC, 0.2% SDS at 65° C.;{'i': 'Aspergillus fumigatus', 'wherein the cellobiohydrolasell or homolog thereof is selected from the group consisting of(i) a cellobiohydrolase II comprising amino acids 20 to 454 of SEQ ID NO: 4;(ii) a cellobiohydrolase II comprising an amino acid sequence having at least 90% sequence identity to amino acids 20 to 454 of SEQ ID NO: 4;(iii) a cellobiohydrolase II encoded by a polynucleotide comprising a nucleotide sequence having at least 90% sequence identity to nucleotides 58 to 1700 of SEQ ...

THERMOSTABLE CELLOBIOHYDROLASE

A thermostable cellobiohydrolase, having a cellobiohydrolase catalytic domain including: (A) a polypeptide including the amino acid sequence represented by SEQ ID NO: 1 or 2, (B) a polypeptide including an amino acid sequence in which at least one amino acid has been deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1 or 2, and having hydrolysis activity against a substrate of phosphoric acid swollen Avicel at least under conditions of 75° C. and pH 5, or (C) a polypeptide including an amino acid sequence having 60% or greater sequence identity with the amino acid sequence represented by SEQ ID NO: 1 or 2, and having hydrolysis activity against a substrate of phosphoric acid swollen Avicel at least under conditions of 75° C. and pH 5. 1. A thermostable cellobiohydrolase , having a cellobiohydrolase catalytic domain comprising:(A) a polypeptide comprising an amino acid sequence represented by SEQ ID NO: 1 or 2,(B) a polypeptide comprising an amino acid sequence in which at least one amino acid has been deleted, substituted, or added in the amino acid sequence represented by SEQ ID NO: 1 or 2, and having hydrolysis activity against a substrate of phosphoric acid swollen Avicel at least under conditions of 75° C. and pH 5, or(C) a polypeptide comprising an amino acid sequence having 60% or greater sequence identity with the amino acid sequence represented by SEQ ID NO: 1 or 2, and having hydrolysis activity against a substrate of phosphoric acid swollen Avicel at least under conditions of 75° C. and pH 5.2. The thermostable cellobiohydrolase according to claim 1 , which claim 1 , in presence of calcium ions claim 1 , exhibits hydrolysis activity against a substrate of phosphoric acid swollen Avicel at least under conditions of 85° C. and pH 5.3. The thermostable cellobiohydrolase according to claim 1 , which also exhibits xylanase activity.4. A polynucleotide claim 1 , having a region encoding a cellobiohydrolase catalytic domain claim ...

PRODUCTION OF LACTASE ENZYMES USING ALTERED REGULATION STRAINS

The present invention relates to new improved methods for expressing native lactases in their native hosts. Methods for homologous as well as heterologous expression of lactase in lactic acid bacteria with altered expression dynamics are comprised by present invention. 1. A method for producing an enzyme having lactase activity in a lactic acid bacterium , preferably wherein said bacterium carries a mutation in the DNA sequence of the glcK gene encoding a glucokinase protein , wherein the mutation inactivates the glucokinase protein , the method comprising the following steps:a) inoculating the lactic acid bacterium in a suitable growth medium comprising lactose;b) growing the lactic acid bacterium of step a) to a desired density to obtain a first solution comprising the enzyme having lactase activity and bacterial cells from the lactic acid bacterium;c) inactivating and/or disrupting the bacterial cells of the lactic acid bacterium to obtain a second solution;d) optionally processing the second solution to obtain a third solution.2. A method for producing an enzyme having lactase activity , the method comprising the following steps:a) inoculating a lactic acid bacterium, preferably wherein said bacterium carries a mutation in the DNA sequence of the glcK gene encoding a glucokinase protein, wherein the mutation inactivates the glucokinase protein, in a suitable growth medium comprising lactose;b) growing the lactic acid bacterium of step a) to a desired density to obtain a solution comprising the enzyme having lactase activity and bacterial cells of the lactic acid bacterium;c) purifying the enzyme having lactase activity from the solution;d) optionally formulating said enzyme in a suitable formulation.3. A method for producing an enzyme having lactase activity , the method comprising the following steps:a) introducing a DNA sequence encoding the enzyme having lactase activity into a lactic acid bacterium, preferably wherein said bacterium carries a mutation in the ...

Enzyme Formulation for Reducing Salicylate Intolerance

Disclosed is a formulation of the following enzymes: Beta Glucanase, Chymotrypsin, Phytase, Lactase, and Invertase, which has been found to be effective in treating salicylate intolerant people, and causing a significant improvement in a wide variety of pathologies and symptoms, including, but not limited to: stuttering, migraines, ADHD, behavioral deficits, Tourettes disease, seizures, autism (ASD), atrial fibrillation., anxiety, depression, joint pain, cognitive and perceptual disorders, respiratory difficulties and non-diabetic neuropathy. 1. A formulation for treating symptoms of one or more of the following diseases or conditions: stuttering , diabetes-associated neuropathy , migraines , ADHD , Tourette's disease , seizures , autism and atrial fibrillation , comprising the enzymes: Beta Glucanase , Chymotrypsin , Phytase , Lactase and Invertase.2. The formulation of claim 1 , wherein the quantities of the enzymes in the formulation are: Beta Glucanase claim 1 , 200 BGU; Chymotrypsin claim 1 , not less than 3000 USP units; Phytase 30 FTU; Lactase 600 ALU and Invertase 600 INVU.3. The formulation of wherein the Chymotrypsin is derived from porcine and the quantity is 3.0 mg.4. A method for treating symptoms of one or more of the following diseases or conditions: stuttering claim 2 , diabetes-associated neuropathy claim 2 , migraines claim 2 , ADHD claim 2 , Tourette's disease claim 2 , seizures claim 2 , autism and atrial fibrillation claim 2 , comprising administering a formulation including the enzymes: Beta Glucanase claim 2 , Chymotrypsin claim 2 , Phytase claim 2 , Lactase and Invertase.5. The method of wherein the quantities of the enzymes in the formulation are: Beta Glucanase claim 4 , 200 BGU; Chymotrypsin claim 4 , not less than 3000 USP units; Phytase 30 FTU; Lactase 600 ALU and Invertase 600 INVU claim 4 , and the formulation is administered twice per day.6. The method of wherein the Chymotrypsin is derived from porcine and the quantity is 3.0 mg. ...

Method for preparing intracellular enzymes

The present invention addresses the problem of preparing an intracellular enzyme of yeast by a simple method. A pulsed electric field is applied to yeast, and the enzyme extracted into an extracellular solution is recovered.

ANTI-TUMOR MEDICAMENT BASED ON ADENOVIRUS

The invention provides manipulated adenovirus, i.e. a viral particle based on a manipulated adenovirus, for use as a medicament, especially for use in the treatment of tumours. The viral particle of the invention has the advantage of having a preference or specificity for tumour cells, yielding a preferred infection of tumour cells. The viral particle is based on adenovirus, especially type C, preferably serotype 2 (Ad2), more preferably serotype 5 (Ad5), in which the native entire fiber protein, and its coding sequence, respectively, is deleted and replaced by a fusion protein providing specificity for cell surface bound polysialic acid. 1. Adenoviral particle for use in the treatment of a tumour comprising a fusion protein comprising from N-terminus to C-terminus a tail domain of an adenoviral fiber protein and an amino acid sequence of an endosialidase of bacteriophage origin , lacking its bacteriophage attachment domain , wherein the fusion protein specifically binds to polysialic acid.2. Adenoviral particle according to claim 1 , wherein the endosialidase of bacteriophage origin claim 1 , lacking its bacteriophage attachment domain is selected from amino acid sequences having an identity of at least 51% to one of SEQ ID NO: 5 (EndoK1E) claim 1 , SEQ ID NO: 6 (EndoK1F) claim 1 , SEQ ID NO: 7 (EndoNK1) claim 1 , and SEQ ID NO: 8 (Endoφ92).3. Adenoviral particle according to claim 1 , wherein at least 1 pseudo-repeat of SEQ ID NO: 14 is arranged between the tail domain and the endosialidase.4. Adenoviral particle according to claim 1 , wherein the tail domain an amino acid sequence of amino acids 1 to 44 of SEQ ID NO: 4.5. Adenoviral particle according to claim 4 , wherein a flexible linker peptide containing at least 2 repeats of one or more amino acid sequences selected from (PT)P claim 4 , wherein X is 1 to 10 claim 4 , and SN(SEQ ID NO: 17) is arranged N-terminally to the endosialidase and C-terminally to the at least one pseudo-repeat.6. Adenoviral particle ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND MAGNESIUM

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and magnesium or a salt or complex thereof. The invention also relates to the combination of a sulforaphane or a derivative thereof and magnesium or a salt or complex thereof. The invention also relates to the combination of a broccoli extract or powder and magnesium or a salt or complex thereof. The invention provides compositions and methods relating to these combinations. 115-. (canceled)16. An orally administrable composition comprising a broccoli extract or powder and magnesium or a salt or complex thereof.17. The orally administrable composition of claim 16 , wherein the broccoli extract or powder comprises glucoraphanin in an amount of about 1 to about 75% w/w.18. The orally administrable composition of claim 16 , wherein the broccoli extract or powder comprises myrosinase.19. The orally administrable composition of claim 16 , further comprising an enzyme potentiator.20. The orally administration composition of claim 16 , wherein the enzyme potentiator comprises ascorbic acid.21. The orally administrable composition of claim 16 , wherein the composition comprises an enteric-coated dosage form.22. The orally administrable composition of claim 16 , further comprising one or more additional components selected from the group consisting of: vitamin k2 claim 16 , quercetin claim 16 , an aminosugar claim 16 , a glycosaminoglycan claim 16 , avocado/soybean unsaponifiable claim 16 , coffee fruit claim 16 , magnesium claim 16 , silymarin claim 16 , proanthocyanidins claim 16 , ursolic acid claim 16 , curcumin claim 16 , phytosterols claim 16 , phytostanols claim 16 , and maitake claim 16 , shiitake claim 16 , and/or reishi mushroom.23. A method of treating claim 16 , preventing claim 16 , reducing the occurrence of claim 16 , decreasing the symptoms associated with claim 16 , and reducing secondary ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND URSOLIC ACID

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and ursolic acid, a salt, ester, amide, or derivative thereof. The invention also relates to the combination of a sulforaphane or a derivative thereof and ursolic acid, a salt, ester, amide, or derivative thereof. The invention also relates to the combination of a broccoli extract or powder and ursolic acid, a salt, ester, amide, or derivative thereof. The invention provides compositions and methods relating to these combinations. 114-. (canceled)15. An orally administrable composition comprising a broccoli extract or a powder and ursolic acid , a salt , ester , amide or a derivative thereof.16. The orally administrable composition of claim 15 , wherein the broccoli extract or powder comprises glucoraphanin in an amount of about 1% to about 75% w/w.17. The orally administrable composition of claim 15 , wherein the broccoli extract or powder comprises myrosinase.18. The orally administrable composition of claim 15 , further comprising an enzyme potentiator.19. The orally administrable composition of claim 15 , wherein the enzyme potentiator comprises ascorbic acid.20. The orally administrable composition of claim 15 , wherein the composition comprises an enteric-coated dosage form.21. The orally administrable composition of claim 15 , further comprising one or more additional components selected from the group consisting of: quercetin claim 15 , an aminosugar claim 15 , a glycosaminoglycan claim 15 , avocado/soybean unsaponifiable claim 15 , a vitamin claim 15 , coffee fruit claim 15 , magnesium claim 15 , silymarin claim 15 , proanthocyanidins claim 15 , alpha- and beta-glucans claim 15 , curcumin claim 15 , phytosterols claim 15 , phytostanols claim 15 , and maitake claim 15 , shiitake claim 15 , and/or reishi mushroom.22. A method of treating claim 15 , preventing claim 15 , reducing the occurrence ...

Pichia pastoris strains for producing predominantly homogeneous glycan structure

Disclosed herein are novel Pichia pastoris strains for expression of exogenous proteins with substantially homogeneous N-glycans. The strains are genetically engineered to include a mutant OCH1 allele which is transcribed into an mRNA coding for a mutant OCH1 gene product (i.e., α-1,6-mannosyltransferase, or “OCH1 protein”). The mutant OCH1protein contains a catalytic domain substantially identical to that of the wild type OCH1 protein, but lacks an N-terminal sequence necessary to target the OCH1 protein to the Golgi apparatus. The strains disclosed herein are robust, stable, and transformable, and the mutant OCH1 allele and the ability to produce substantially homogeneous N-glycans are maintained for generations after rounds of freezing and thawing and after subsequent transformations.

PRODUCTION OF ENZYMES FOR LIGNO-CELLULOSIC BIOMASS

A process produces at least a first enzyme from a host cell, wherein the first enzyme is capable of hydrolyzing a first pre-treated ligno-cellulosic biomass. The process comprises the step of cultivating the host cell to produce at least the first enzyme for a cultivation time, wherein the cultivation of the host cell occurs in a sugar depleted cultivation environment comprising the host cell, water and a solid composition comprising a complex sugar of the solid composition and a lignin of the solid composition. In such a process, the solid composition is obtained from a second pre-treated ligno-cellulosic biomass, comprising a complex sugar of the second pre-treated ligno-cellulosic biomass and a lignin of the second pre-treated ligno-cellulosic biomass; and the ratio of the total amount of the complex sugars of the solid composition to the total amount of the lignin of the solid composition is greater than zero and less than the ratio of the total amount of the complex sugars of the second pre-treated ligno-cellulosic biomass to the total amount of the lignin of the second pre-treated ligno-cellulosic biomass. 119-. (canceled)20. A process which produces at least a first enzyme from a host cell , wherein the first enzyme is capable of hydrolyzing a first pre-treated ligno-cellulosic biomass ,said process comprising the step of cultivating the host cell to produce at least the first enzyme for a cultivation time, wherein a) the solid composition is obtained from a second pre-treated ligno-cellulosic biomass, comprising a complex sugar of the second pre-treated ligno-cellulosic biomass and a lignin of the second pre-treated ligno-cellulosic biomass; and', 'b) the ratio of the total amount of the complex sugars to the total amount of the lignin in the solid composition is less than the ratio of the total amount of the complex sugars to the total amount of the lignin in the second pre-treated ligno-cellulosic biomass., 'the cultivation of the host cell occurs in a ...

Polypeptides Having Beta-1,3-Galactanase Activity and Polynucleotides Encoding Same

The present invention relates to polypeptides having beta-1,3-galactanase activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. A polypeptide having beta-1 ,3-galactanase activity , selected from the group consisting of:(a) a polypeptide having at least 65% sequence identity to the mature polypeptide of SEQ ID NO: 2;(b) a polypeptide encoded by a polynucleotide that hybridizes under low stringency conditions with the mature polypeptide coding sequence of SEQ ID NO: 1 or the full-length complement hereof;(c) a polypeptide encoded by a polynucleotide having at least 65% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1;(d) a variant of the mature polypeptide of SEQ ID NO: 2 comprising a substitution, deletion, and/or insertion at one or more positions; and(e) a fragment of the polypeptide of (a), (b), (c), or (d) that has beta-1,3-galactanase activity.2. The polypeptide of claim 1 , which is an isolated polypeptide.3. The polypeptide of claim 1 , having at least 65% sequence identity to the mature polypeptide of SEQ ID NO: 2.4. The polypeptide of claim 1 , which is encoded by a polynucleotide that hybridizes under low stringency conditions claim 1 , low-medium stringency conditions claim 1 , medium stringency conditions claim 1 , medium-high stringency conditions claim 1 , high stringency conditions claim 1 , or very high stringency conditions with the mature polypeptide coding sequence of SEQ ID NO: 1 or the full-length complement hereof.5. The polypeptide of claim 1 , which is encoded by a polynucleotide having at least 65% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1.6. The polypeptide of claim 1 , comprising or consisting of SEQ ID NO: 2 or the mature polypeptide of SEQ ID NO: 2.7. The polypeptide of claim 1 , wherein the mature ...

DELIVERING ENZYME USING AN INJECTABLE HYDROGEL DEPOT

Compositions and methods for delivering enzymes in enzyme hydrogel formulations are disclosed. More particularly, the present disclosure relates to injectable enzyme hydrogel formulations and delivery of injectable enzyme hydrogel formulations. Also disclosed are methods for GALNS enzyme replacement therapy and lysosomal enzyme replacement therapy. 1. A method of administering to an individual in need thereof an enzyme replacement therapy in an injectable enzyme hydrogel formulation , wherein the injectable enzyme hydrogel formulation is not a microparticle , the method comprising:preparing an injectable enzyme hydrogel formulation by mixing an enzyme, a polymer, and a buffer solution to form a precursor solution;initiating polymerization of the precursor solution to form the injectable enzyme hydrogel formulation; andadministering the enzyme hydrogel formulation to the individual in need thereof.2. The method of claim 1 , further comprising monitoring polymerization of the injectable enzyme hydrogel formulation.3. The method of claim 1 , further comprising introducing the injectable enzyme hydrogel formulation into an applicator.4. The method of claim 1 , wherein the enzyme is selected from the group consisting of N-acetylgalactosamine 6-sulfate sulfatase (GALNS) and a lysosomal enzyme selected from the group consisting of Iduronate-2-sulfate sulfatase claim 1 , Heparan N sulfatase claim 1 , N-acetylglucosaminidase claim 1 , acetyl-CoA: glucosaminide acetyltransferase claim 1 , N-acetylglucosamine 6-sulfatase claim 1 , Arylsulfatase B claim 1 , Glucuronidase claim 1 , acid glucosidase claim 1 , and combinations thereof.5. The method of claim 1 , wherein the enzyme comprises a recombinant enzyme.6. The method of claim 1 , wherein the enzyme comprises a human enzyme.7. The method of claim 1 , wherein the polymer comprises polyethylene glycol (PEG) claim 1 , polyethylene glycol acrylate (PEGAc) claim 1 , poly(glycolic acid) (PGA) claim 1 , poly(L-lactic acid) (PLA) ...

Polypeptides Having Glucoamylase Activity and Polynucleotides Encoding Same

The present invention relates to isolated polypeptides having glucoamylase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides. 1. An isolated polypeptide having glucoamylase activity , selected from the group consisting of:(a) a polypeptide comprising an amino acid sequence having preferably at least 72%, more preferably at least 73%, more preferably at least 74%, more preferably at least 75%, more preferably at least 76%, more preferably at least 77%, more preferably at least 78%, more preferably at least 79%, more preferably at least 80%, more preferably at least 81%, more preferably at least 82%, more preferably at least 83%, more preferably at least 84%, more preferably at least 85%, more preferably at least 86%, more preferably at least 87%, more preferably at least 88%, more preferably at least 89%, more preferably at least 90%, more preferably at least 91%, more preferably at least 92%, even more preferably at least 93%, most preferably at least 94%, and even most preferably at least 95%, such as at least 95%, at least 97%, at least 98%, at least 99% or even 100% identity to the mature polypeptide of SEQ ID NO: 2;(b) a polypeptide comprising an amino acid sequence having preferably at least 72%, more preferably at least 73%, more preferably at least 74%, more preferably at least 75%, more preferably at least 76%, more preferably at least 77%, more preferably at least 78%, more preferably at least 79%, more preferably at least 80%, more preferably at least 81%, more preferably at least 82%, more preferably at least 83%, more preferably at least 84%, more preferably at least 85%, more preferably at least 86%, more preferably at least 87%, more preferably at least 88%, more preferably at least 89%, more preferably at least 90%, more preferably at least 91%, more preferably at least ...

IMPROVED BACILLUS HOST

The invention provides host cell deficient in the production of a neutral protease and of a alkaline protease which host cell comprises a nucleic acid construct, wherein the nucleic acid construct comprises a polynucleotide encoding a compound of interest or encoding a compound involved in the synthesis of a compound of interest operably linked to a promoter sequence allowing for expression of the polynucleotide in the host cell, wherein the promoter comprises a bacteriophage promoter sequence, more preferably a bacteriophage SPO1 promoter sequence. Said host cell can advantageously be used in a method of production of a compound of interest. 1Bacillus. A recombinant host cell deficient in the production of a neutral protease and/or of an alkaline protease which host cell comprises a nucleic acid construct , wherein the nucleic acid construct comprises a polynucleotide encoding a compound of interest or encoding a compound involved in the synthesis of a compound of interest operably linked to a promoter sequence allowing for expression of the polynucleotide in the host cell , wherein the promoter comprises a bacteriophage SPO1 promoter sequence , preferably a bacteriophage SPO1 promoter sequence which comprises a polynucleotide sequence according to SEQ ID NO: 36 or a polynucleotide sequence at least 70% identical to SEQ ID NO: 36.2Bacillus. Method of producing a recombinant host cell according to comprising:{'i': 'Bacillus', 'a. providing a host cell deficient in the production of a neutral protease and/or in the production of an alkaline protease, preferably deficient in the production of a neutral α-amylase, preferably deficient in a sporulation-related gene;'}{'i': 'Bacillus', 'b. transforming the host cell with a nucleic acid construct comprising a polynucleotide encoding a compound of interest or encoding a compound involved in the synthesis of a compound of interest operably linked to a promoter sequence allowing for expression of the polynucleotide in the ...

COMPOSITIONS AND METHODS FOR TREATING EYE INFECTIONS AND DISEASE

The present invention provides compositions and methods for identifying subjects suffering from dry eye that can be treated by topical administration of a composition comprising lacritin or a bioactive fragment thereof. The application discloses in part that a ˜90 KDa deglycanated form of syndecan-1 is abundant in tears of normal individuals but not individuals suffering from dry eye, whereas a ˜25 kDa syndecan-1 fragment is detectable in dry, but no normal tears. 1. A method for identifying a subject having dry eye , said method comprising 90 kDa deglycanated SDC-1;', '25 kDa SDC-1; and', 'inactive lacritin-C splice variant;, 'detecting the presence of at least one protein selected from the group consisting of latent heparanase;'}in a tear sample obtained from said subject, whereina decreased level of latent heparanase or increase in active heparanase, relative to levels present in tears from a normal eye;a decreased level of 90 kDa deglycanated SDC-1, relative to levels present in tears from a normal eye;detection of 25 kDa SDC-1; and/ordetection of inactive lacritin-C splice variant identifies subjects having dry eye.2. The method of wherein the concentration of 90 kDa deglycanated SDC-1 and 25 kDa SDC-1 are measured in a tear sample obtained from said subject wherein decreased levels of 90 kDa deglycanated SDC-1 coupled with increased levels of 25 kDa SDC-1 relative to levels present in tears from a normal eye identifies subjects having dry eye.3. The method of wherein a tear sample obtained from said subject is screened for the presence of 25 kDa SDC-1 claim 1 , wherein detection of 25 kDa SDC-1 identifies a subject having dry eye.4. The method of wherein a tear sample obtained from said subject is screened for the presence of inactive lacritin-C splice variant claim 1 , wherein detection of inactive lacritin-C splice variant identifies a subject having dry eye.5. The method of wherein a tear sample obtained from said subject is screened for the presence of 25 ...

NOVEL METHOD FOR PURIFYING 3,6-ANHYDRO-L-GALACTOSE BY USING MICROORGANISMS

The present invention relates to a novel method for purifying 3,6-anhydro-L-galactose by using microorganisms and provides an effect of improving the production yield of 3,6-anhydro-L-galactose by using microorganisms during purification after enzymatic hydrolysis of agarose or agar. 1. A method for purifying 3 ,6-anhydro-L-galactose using microorganisms , comprising:reacting a group of enzymes including a thermostable agarase represented by an amino acid sequence set forth in SEQ ID NO: 1, an exo-type agarase and an α-neoagarobiose hydrolase with agarose or agar as a substrate;culturing a microorganism having an ability to metabolize galactose using a product obtained from the above reaction as a carbon source; andobtaining 3,6-anhydro-L-galactose from a culture of the microorganism.2. The method according to claim 1 , wherein the reaction between the group of enzymes and the substrate is performed without pretreatment of agarose or agar.3. The method according to claim 1 , wherein the reaction between the group of enzymes and the substrate includes reacting a thermostable agarase with agarose or agar claim 1 , and reacting a product obtained from the above reaction with an exo-type agarase and an α-neoagarobiose hydrolase.4. The method according to claim 3 , wherein the reaction between the thermostable agarase and the agarose or agar is performed at a temperature ranging from 40 to 60° C. under a condition of 0 to 300 rpm and a pH ranging from 5 to 9 for 30 minutes to 7 days.5. The method according to claim 3 , wherein the exo-type agarase is represented by an amino acid sequence set forth in SEQ ID NO: 3.6. The method according to claim 3 , wherein the α-neoagarobiose hydrolase is represented by an amino acid sequence set forth in SEQ ID NO: 4.7. The method according to claim 3 , wherein reactions with the exo-type agarase and the α-neoagarobiose hydrolase are performed at a temperature ranging from 20 to 40° C. claim 3 , under a condition of 0 to 200 rpm claim ...

ENZYME PREPARATIONS YIELDING A CLEAN TASTE

The present invention describes a intracellular produced lactase, which comprises less than 40 units arylsulfatase activity per NLU of lactase activity. The invention also provides a process comprising treating a substrate with an enzyme preparation, wherein the enzyme preparation is substantially free from arylsulfatase. 1. A lactase which comprises less than 40 units arylsulfatase activity per NLU of lactase activity.2. The lactase according to claim 1 , which comprises less than 10 units arylsulfatase activity per NLU of lactase activity.3. The lactase according to claim 1 , which is an intracellular produced lactase.4. The lactase according to claim 1 , which is a neutral lactase.5K. lactis. The lactase according to claim 4 , which is a lactase.6. The lactase according to claim 1 , which has a pH optimum of between pH=6 and pH=8.7. The lactase according to claim 1 , which has less than 0.5 RFU/min protease activity per NLU of lactase activity.8. A composition comprising the lactase of .9. A dairy product comprising the lactase of .10. A process to produce a dairy product which comprises adding a lactase of to a dairy product which comprises lactose.11. A process to produce a dairy product which is free of off flavours produced by arylsulfatase which comprises using a lactase of .12. A process to purify a lactase-containing enzyme preparation claim 1 , which comprises separation of aryl-sulfatase from lactase using chromatography.13. A process comprising treating a substrate with an enzyme preparation claim 1 , wherein the enzyme preparation is substantially free from arylsulfatase.14. A process for preparing an enzyme preparation claim 1 , said process comprising purifying a crude enzyme preparation which contains an enzyme of interest and arylsulfatase claim 1 , wherein arylsulfatase is separated from the enzyme of interest.15. A process comprising treating a substrate with an enzyme preparation obtained by a process of .16. The process according to claim 15 , ...

An enzyme exhibiting fructan hydrolase activity

The present invention is related to an enzyme that allows efficient removal of fructan from grain and vegetable raw material. The enzyme according to the invention produces grain and vegetable material having a fructan content significantly lower compared to that of the starting material. 1. A DNA construct comprising a nucleotide sequence encoding an extracellular fructosidase , wherein said nucleotide sequence comprises the nucleotide sequence shown in SEQ ID No. 1 or an analogous sequence thereof having at least 96% identity to the nucleotide sequence shown in SEQ ID No. 1.2Lactobacillus.. The DNA construct according to claim 1 , wherein the nucleotide sequence encoding an extracellular fructosidase is obtainable from a strain of3Lactobacillus,Lactobacillus crispatus, Lactobacillus helveticus, Lactobacillus amylovorus, Lactobacillus ultunensis, Lactobacillus amylolyticus, Lactobacillus amylovorans, Lactobacillus sobriusLactobacillus acidophilus.. The DNA construct according to claim 2 , wherein the nucleotide sequence is obtainable from a strain of in particular a strain of or4Lactobacillus crispatus. The DNA construct according to claim 3 , wherein the nucleotide sequence is obtainable from (DSM 29598).5. A recombinant expression vector comprising a DNA construct claim 3 , wherein the DNA construct comprises a nucleotide sequence encoding an extracellular fructosidase claim 3 , wherein said nucleotide sequence comprises the nucleotide sequence shown in SEQ ID No. 1 or an analogous sequence thereof having at least 96% identity to the nucleotide sequence shown in SEQ ID No 1.6. A cell comprising a recombinant expression vector claim 3 , wherein the recombinant expression vector comprises a DNA construct and .wherein the DNA construct comprises a nucleotide sequence encoding an extracellular fructosidase wherein said nucleotide sequence comprises the nucleotide sequence shown in SEQ ID No. 1 or an analogous sequence thereof having at least 96% identity to the ...

Novel xylanase

Provided is a novel xylanase having high xylanase activity. A protein consisting of an amino acid sequence described in the following (a), (b) or (c) and having xylanase activity: (a) the amino acid sequence set forth in positions 23 to 404 of SEQ ID NO: 2; (b) an amino acid sequence having at least 90% identity to the amino acid sequence set forth in positions 23 to 404 of SEQ ID NO: 2; (c) an amino acid sequence modified from the amino acid sequence set forth in positions 23 to 404 of SEQ ID NO: 2 by deletion, insertion, substitution, or addition of one or more amino acids.

Broccoli Based Nutritional Supplements

A nutritional supplement is provided containing two broccoli based components that are combined and, when ingested, react in the intestines to provide sulforaphane. Processes for producing the broccoli components of the nutritional supplement are also provided. The broccoli components are treated separately using supercritical fluid extraction to remove oils. The temperature and pressure of the supercritical extraction processes are controlled to provide broccoli components having the desired properties for the nutritional supplement.

COMPOSITIONS AND METHODS FOR TREATING EYE INFECTIONS AND DISEASE

The present invention provides compositions and methods for identifying subjects suffering from dry eye that can be treated by topical administration of a composition comprising lacritin or a bioactive fragment thereof. The application discloses in part that a ˜90 KDa deglycanated form of syndecan-1 is abundant in tears of normal individuals but not individuals suffering from dry eye, whereas a ˜25 kDa syndecan-1 fragment is detectable in dry, but not normal tears. 120-. (canceled)21. A bactericidal composition , comprising a C-terminal fragment of lacritin selected from SEQ ID NO: 7 , or SEQ ID NO: 8 , or a derivative thereof that differs from SEQ ID NO: 7 or SEQ ID NO: 8 by one or two amino acid substitutions; and a pharmaceutically acceptable carrier; wherein the composition is suitable for topical administration to an ocular surface of a subject.22. The composition of wherein the amino acid substitutions are located at positions 4 claim 21 , 6 claim 21 , 8 claim 21 , 10 claim 21 , 17 and 19 relative to the numbering of SEQ ID NO: 7.23. The composition of wherein the C-terminal fragment of lacritin consists of SEQ ID NO: 7.24. The composition of claim 21 , wherein the composition claim 21 , further comprises a second anti-bacterial agent.25. The composition of claim 24 , wherein the second anti-bacterial agent is lysozyme.26. The composition of claim 25 , wherein the weight ratio of lysozyme to the C-terminal fragment of lacritin is from 4:1 to 3:1.27. A method of treating a corneal infection claim 21 , said method comprising selecting a subject having a corneal infection and contacting the cornea of the subject with the composition of . This application is a continuation of U.S. application Ser. No. 15/125,357, filed Sep. 12, 2016, which is a U.S. national counterpart application of PCT International Application Serial No. PCT/US2015/019964, filed Mar. 11, 2015, which claims priority to U.S. Provisional Application Ser. No. 62/019,476, filed Jul. 1, 2014, and U. ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND A MILK THISTLE EXTRACT OR POWDER

The invention relates to the combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, an enzyme potentiator, and a milk thistle extract or powder. The invention also relates to the combination of a sulforaphane or a derivative thereof and a milk thistle extract or powder. The invention also relates to the combination of a broccoli extract or powder and a milk thistle extract or powder. The invention provides compositions and methods relating to these combinations. 114-. (canceled)15. An orally administrable composition comprising a broccoli extract or powder and a milk thistle extract or powder.16. The orally administrable composition of claim 15 , wherein the broccoli extract or powder comprises glucoraphanin in an amount of about 1 to about 75% w/w.17. The orally administrable composition of claim 15 , wherein the broccoli extract or powder comprises myrosinase.18. The orally administrable composition of claim 15 , further comprising an enzyme potentiator.19. The orally administrable composition of claim 15 , wherein the enzyme potentiator comprises ascorbic acid.20. The orally administrable composition of claim 15 , wherein the composition comprises an enteric-coated dosage form.21. The orally administrable composition of claim 15 , comprising a milk thistle extract comprising silymarin.22. The orally administrable composition of claim 15 , comprising a milk thistle extract comprising silibinin.23. The orally administrable composition of claim 15 , further comprising one or more additional components selected from the group consisting of: quercetin claim 15 , an aminosugar claim 15 , a glycosaminoglycan claim 15 , avocado/soybean unsaponifiable claim 15 , a vitamin claim 15 , coffee fruit claim 15 , magnesium claim 15 , silymarin claim 15 , proanthocyanidins claim 15 , ursolic acid claim 15 , curcumin claim 15 , phytosterols claim 15 , phytostanols claim 15 , and S-adenosylmethionine (SAMe).24. A method ...

Biofumigant

A method of treating soil, the method comprising providing the soil with a glucosinolate-secreting plant or a source thereof and contacting said soil with a myrosinase-secreting yeast of the x or a source thereof.

METHODS OF COMBINED BIOPROCESSING AND RELATED MICROORGANISMS, THERMOPHILIC AND/OR ACIDOPHILIC ENZYMES, AND NUCLEIC ACIDS ENCODING SAID ENZYMES

A genetically modified organism comprising: at least one nucleic acid sequence and/or at least one recombinant nucleic acid isolated from and encoding a polypeptide involved in at least partially degrading, cleaving, transporting, metabolizing, or removing polysaccharides, cellulose, lignocellulose, hemicellulose, lignin, starch, sugars, sugar oligomers, carbohydrates, complex carbohydrates, chitin, heteroxylans, glycosides, xylan-, glucan-, galactan-, or mannan-decorating groups; and at least one nucleic acid sequence and/or at least one recombinant nucleic acid encoding a polypeptide involved in fermenting sugar molecules to a product. Additionally, enzymatic and/or proteinaceous extracts may be isolated from one or more genetically modified organisms. The extracts are utilized to convert biomass into a product. Further provided are methods of converting biomass into products comprising: placing the genetically modified organism and/or enzymatic extracts thereof in fluid contact with polysaccharides, cellulose, lignocellulose, hemicellulose, lignin, starch, sugars, sugar oligomers, carbohydrates, complex carbohydrates, chitin, heteroxylans, glycosides, and/or xylan-, glucan-, galactan-, or mannan-decorating groups. 1. A genetically modified bacterial or fungal organism , the genetically modified organism comprising:{'i': 'Alicyclobacillus acidocaldarius', 'at least one exogenous nucleic acid isolated from and encoding a polypeptide having at least 90% homology to SEQ ID NO:337 and wherein the peptide has alpha-glucuronidase activity; and'}at least one nucleic acid sequence encoding a polypeptide associated with fermenting sugar molecules to a product.2Alicyclobacillus acidocaldarius. The genetically modified organism of claim 1 , wherein the at least one exogenous nucleic acid from is integrated into the host organism's genome.3. The genetically modified organism of claim 1 , wherein the polypeptide has alpha-glucuronidase activity at or above fifty degrees ...

Structured Liquid Compositions

Microfibrillated cellulose, derived from vegetables or wood, can be used to provide a liquid composition which is compatible with a broad range of ingredients suitable for consumer applications, including enzymes, while still providing good structuring of the liquid composition, without affecting ease of pour. 1. A liquid composition comprising:a) surfactant,b) microfibrillated cellulose derived from wood, andc) enzymes selected from the group consisting of: cellulases, endoglucanase with activity towards xyloglucan, and mixtures thereof.2. The composition according to claim 1 , wherein the surfactant is selected from the group consisting of: anionic surfactant claim 1 , nonionic surfactant claim 1 , cationic surfactant claim 1 , and mixtures thereof.3. The composition according to claim 1 , wherein the composition comprises from about 0.5% to about 40 wt % of the surfactant.4. The composition according to claim 1 , wherein the microfibrillated cellulose has an aspect ratio (l/d) of from about 50 to about 200 claim 1 ,000.5. The composition according to claim 1 , wherein the microfibrillated cellulose is derived from wood claim 1 , wherein the wood comprises less than about 10% soluble fibre as a percentage of total fibre.6. (canceled)7. The composition according to claim 1 , wherein the composition comprises from about 0.05 to about 10 wt % of the microfibrillated cellulose.8. The composition according to claim 1 , wherein the composition comprises sufficient microfibrillated cellulose to provide a yield stress of greater than about 0.005 Pa.9. (canceled)10. The composition according to claim 1 , wherein the composition further comprises a suspended insoluble material.11. A liquid composition comprising:a) surfactant, andb) microfibrillated cellulose derived from wood,wherein the composition further comprises a water-soluble polymer.12. The composition according to claim 11 , wherein the water-soluble polymer is selected from carboxylate polymers claim 11 , ...

DESIGNER alpha 6-FUCOSIDASE MUTANTS ENABLE DIRECT CORE FUCOSYLATION OF INTACT N-GLYCOPEPTIDES AND N-GLYCOPROTEINS

The present invention provides for novel fucosidase mutants that server as fuco-ligases for core fucosylation of a range of biological glycopeptides and glycoproteins including intact therapeutic antibodies. Several mutants with mutation at the general acid/base residue E274 of the α1,6-fucosidase, including E274A, E274S, and E274G, were able to efficiently fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins. The site specific mutants enable the transfer of fucose to a core GlcNAc-Asn residue and useful for drug delivery and vaccine development. 2. The catalytic method according to claim 1 , wherein the activated glycosyl donor is selected from the group consisting of α-fucosyl fluoride αFucF claim 1 , α-fucosyl chloride claim 1 , α-fucosyl azide claim 1 , 4-nitrophenyl α-fucoside claim 1 , 3-nitrophenyl α-fucoside claim 1 , 3 claim 1 ,4-dinitrophenyl α-fucoside claim 1 , and 4-methylumbelliferyl α-fucoside.3Lactobacillus casei. The catalytic method according to claim 1 , wherein α1 claim 1 ,6-fucosidase mutant enzyme is selected from the group comprising E274A claim 1 , E274S claim 1 , E274G claim 1 , E274T claim 1 , E274C claim 1 , E274I claim 1 , E274L claim 1 , E274M claim 1 , E274F claim 1 , E274W claim 1 , E274Y and E274V or mutants having at least 90% homology thereof with fucosylating activity and derived from fucosidase (AlfC).4Lactobacillus casei. The catalytic method according to claim 1 , wherein α1 claim 1 ,6-fucosidase mutant enzyme is selected from a group comprising E274A (SEQ ID NO: 1) claim 1 , E274S (SEQ ID NO: 2) and E274G (SEQ ID NO:3) derived from α-fucosidase (SEQ ID NO: 4).5. The catalytic method according to claim 4 , further comprising CPD and HIS (SEQ ID NO: 31) or CPD (SEQ ID NO. 30).6. A chemoenzymatic method for the preparation of homogeneous fucosylated glycopeptides or glycoproteins claim 4 , comprising:providing an nonfucosylated glycopeptide or glycoprotein acceptor; and{'i': 'Lactobacillus casei', ' ...

ENZYME PREPARATIONS YIELDING A CLEAN TASTE

The present invention describes a intracellular produced lactase, which comprises less than 40 units arylsulfatase activity per NLU of lactase activity. The invention also provides a process comprising treating a substrate with an enzyme preparation, wherein the enzyme preparation is substantially free from arylsulfatase. 1. A process for producing a dairy product which comprises adding a lactase obtained from yeast to a dairy product comprising lactose , wherein said lactase comprises less than 30 units arylsulfatase activity per NLU of lactase activity.2. The process of wherein the dairy product produced is free of off-flavours produced by arylsulfatase.3. The process according to claim 2 , wherein said dairy product contains an alkyl phenol substituted with a sulfate group.4. The process according to claim 2 , wherein the dairy product contains milk protein.5. The process according to claim 2 , wherein the dairy product is selected from the group consisting of milk and a fermented milk product.6. The process according to claim 2 , wherein the level of arylsulfatase in the dairy product during said treating is at most 500*10E3 arylsulfatase units per liter of dairy product.7. A dairy product obtainable by the process according to .8. The process according to claim 4 , wherein the milk protein is selected from the group consisting of casein and whey protein.9. The process according to claim 5 , wherein the fermented milk product is yoghurt claim 5 , whey or a hydrolysate.10. The process according to claim 6 , wherein the level of arylsulfatase in the dairy product during said treating is at most 250*10E3 arylsulfatase units per liter of dairy product.11. The process according to claim 10 , wherein the level of arylsulfatase in the dairy product during said treating is at most 100*10E3 arylsulfatase units per liter of dairy product.12. The process according to claim 10 , wherein the level of arylsulfatase in the dairy product during said treating is at most 50*10E3 ...

CLEANING COMPOSITIONS AND USES THEREOF

The present invention relates to compositions such as cleaning compositions comprising a mix of enzymes. The invention further relates, use of compositions comprising such enzymes in cleaning processes and/or for deep cleaning of organic soiling, methods for removal or reduction of components of organic matter. 1. A cleaning composition comprising a DNase , a Glyco_hydro_114 glycosyl hydrolase and a cleaning component.2. A cleaning composition according to claim 1 , wherein the DNase is microbial claim 1 , preferably obtained from bacteria or fungi.3BacillusBacillusBacillus horikoshii, Bacillus licheniformis, Bacillus subtilis, Bacillus horneckiae, Bacillus idriensis, Bacillus algicola, Bacillus vietnamensis, Bacillus hwajinpoensis, Bacillus indicus, Bacillus marisflaviBacillus luciferensis.. A cleaning composition according to claim 2 , wherein the DNase is obtained from claim 2 , preferably cibi claim 2 , or4. A cleaning composition of claim 3 , wherein the DNase comprises one or both of the motif(s) [D/M/L][S/T]GYSR[D/N] (SEQ ID NO: 73) or ASXNRSKG (SEQ ID NO: 74).5. A cleaning composition according to claim 2 , wherein the DNase has at least 60% claim 2 , at least 65% claim 2 , at least 70% claim 2 , at least 75% claim 2 , at least 80% claim 2 , at least 85% claim 2 , at least 90% claim 2 , at least 95% claim 2 , at least 98% claim 2 , at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO 13.6. A cleaning composition according to claim 2 , wherein the DNase has at least 60% claim 2 , at least 65% claim 2 , at least 70% claim 2 , at least 75% claim 2 , at least 80% claim 2 , at least 85% claim 2 , at least 90% claim 2 , at least 95% claim 2 , at least 98% claim 2 , at least 99% or 100% sequence identity to the amino acid sequence shown in SEQ ID NO: 65.7. A cleaning composition according to claim 2 , wherein the DNase has at least 60% claim 2 , at least 65% claim 2 , at least 70% claim 2 , at least 75% claim 2 , at least 80% claim 2 ...

PICHIA PASTORIS STRAINS FOR PRODUCING PREDOMINANTLY HOMOGENEOUS GLYCAN STRUCTURE

Disclosed herein are novel strains for expression of exogenous proteins with substantially homogeneous N-glycans. The strains are genetically engineered to include a mutant OCH1 allele which is transcribed into an mRNA coding for a mutant OCH1 gene product (i.e., α-1,6-mannosyltransferase, or “OCH1 protein”). The mutant OCH1protein contains a catalytic domain substantially identical to that of the wild type OCH1 protein, but lacks an N-terminal sequence necessary to target the OCH1 protein to the Golgi apparatus. The strains disclosed herein are robust, stable, and transformable, and the mutant OCH1 allele and the ability to produce substantially homogeneous N-glycans are maintained for generations after rounds of freezing and thawing and after subsequent transformations. 116.-. (canceled)17Pichia pastoris. An engineered strain of , comprising:a mutant OCH1 allele which is transcribed into a mRNA coding for a mutant OCH1 protein,wherein said mutant OCH1 protein comprises a catalytic domain that (i) comprises residues 45-404 of the wild type OCH1 protein of the amino acid sequence of SEQ ID NO: 2, or (ii) is at least 90% identical to the amino acids corresponding to residues 45-404 of the wild type OCH1 protein of SEQ ID NO: 2 and has α-1, 6-mannosyltransferase activity;wherein said mutant OCH1 protein lacks an N-terminal sequence for targeting the mutant OCH1 protein to the Golgi apparatus; andwherein said engineered strain has a mutant his gene.18. The strain of claim 17 , wherein the mutant his gene is a mutant his4 gene.19. The strain of claim 17 , wherein the mutant OCH1 protein lacks a membrane anchor domain at the N-terminal region.20. The strain of claim 17 , wherein said mutant OCH1 protein comprises the amino acid sequence as set forth in SEQ ID NO: 3.21. The strain of claim 17 , wherein said mutant OCH1 allele is present on a chromosome.22. The strain of claim 21 , wherein said mutant OCH1 allele replaces the wild type OCH1 allele at the OCH1 locus.23. The ...

COMPOSITIONS COMPRISING SULFORAPHANE OR A SULFORAPHANE PRECURSOR AND A MUSHROOM EXTRACT OR POWDER

The present disclosure relates to the synergistic combination of a sulforaphane precursor, an enzyme capable of converting the sulforaphane precursor to sulforaphane, a cofactor of the enzyme, and a glucan. The present disclosure also relates to the synergistic combination of sulforaphane or a derivative thereof and a glucan. The present disclosure also relates to the synergistic combination of a broccoli extract or powder and a glucan. The glucan may be a β-glucan. The glucan may be provided in a mushroom extract or powder selected from one or more of a maitake, a shiitake, or a reishi mushroom. Compositions and methods relating to these combinations are described. 1. An orally administrable composition comprising a synergistic combination of:a sulforaphane precursor;a glucosidase enzyme capable of converting the sulforaphane precursor to sulforaphane;a glucosidase enzyme cofactor; anda glucan.2. The orally administrable composition of claim 1 , wherein the sulforaphane precursor comprises glucoraphanin claim 1 , the glucosidase enzyme comprises myrosinase claim 1 , and the glucosidase enzyme cofactor comprises ascorbic acid.3. The orally administrable composition of claim 1 , wherein the composition comprises an enteric-coated dosage form.4. The orally administrable composition of claim 1 , wherein the composition comprises a mushroom extract or powder comprising the glucan.5. The orally administrable composition of claim 1 , wherein the composition comprises a yeast extract or powder comprising the glucan.6. The orally administrable composition of claim 1 , wherein the glucan is a β-glucan.7. The orally administrable composition of claim 4 , wherein the mushroom extract or powder is derived from one or more of a maitake mushroom claim 4 , a shiitake mushroom claim 4 , and a reishi mushroom.8. The orally administrable composition of claim 5 , wherein the yeast extract or powder is derived from a Baker's yeast.9. The orally administrable composition of claim 1 , ...

Enzyme Compositions and Uses Thereof

The present invention relates to enzyme compositions and processes of producing and using the compositions for the saccharification of lignocellulosic material. 1. An enzyme composition , comprising: (A) (i) a cellobiohydrolase I , (ii) a cellobiohydrolase II , and (iii) at least one enzyme selected from the group consisting of a beta-glucosidase or a variant thereof , an AA9 polypeptide having cellulolytic enhancing activity , a GH10 xylanase , and a beta-xylosidase; (B) (i) a GH10 xylanase and (ii) a beta-xylosidase; or (C) (i) a cellobiohydrolase I , (ii) a cellobiohydrolase II , (iii) a GH10 xylanase , and (iv) a beta-xylosidase;wherein the cellobiohydrolase I is selected from the group consisting of: (i) a cellobiohydrolase I comprising or consisting of the mature polypeptide of SEQ ID NO: 2; (ii) a cellobiohydrolase I comprising or consisting of an amino acid sequence having at least 70% sequence identity to the mature polypeptide of SEQ ID NO: 2; (iii) a cellobiohydrolase I encoded by a polynucleotide comprising or consisting of the mature polypeptide coding sequence of SEQ ID NO: 1; (iv) a cellobiohydrolase I encoded by a polynucleotide comprising or consisting of a nucleotide sequence having at least 70% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 1; and (v) a cellobiohydrolase I encoded by a polynucleotide that hybridizes under at least high stringency conditions with the mature polypeptide coding sequence of SEQ ID NO: 1 or the full-length complement thereof;wherein the cellobiohydrolase II is selected from the group consisting of: (i) a cellobiohydrolase II comprising or consisting of the mature polypeptide of SEQ ID NO: 4; (ii) a cellobiohydrolase II comprising or consisting of an amino acid sequence having at least 70% sequence identity to the mature polypeptide of SEQ ID NO: 4; (iii) a cellobiohydrolase II encoded by a polynucleotide comprising or consisting of the mature polypeptide coding sequence of SEQ ID NO: 3; (iv) ...

THERMOPHILIC AND THERMOACIDOPHILIC BIOPOLYMER-DEGRADING GENES AND ENZYMES FROM ALICYCLOBACILLUS ACIDOCALDARIUS AND RELATED ORGANISMS, METHODS

Isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from are provided. Further provided are methods of at least partially degrading, cleaving, or removing polysaccharides, lignocellulose, cellulose, hemicellulose, lignin, starch, chitin, polyhydroxybutyrate, heteroxylans, glycosides, xylan-, glucan-, galactan-, or mannan-decorating groups using isolated and/or purified polypeptides and nucleic acid sequences encoding polypeptides from 16-. (canceled)7. A method of at least partially degrading , cleaving , or removing polysaccharides , lignocellulose , cellulose , hemicellulose , lignin , starch , chitin , polyhydroxybutyrate , heteroxylans , glycosides , xylan , glucan , galactan , or mannan decorating groups , the method comprising:placing a polypeptide at least 90% sequence identity to SEQ ID No. 287 in fluid contact with a polysaccharide, lignocellulose, cellulose, hemicellulose, lignin, starch, chitin, polyhydroxybutyrate, heteroxylans, glycoside, xylan, glucan, galactan, or mannan decorating group;wherein the polypeptide has an enzymatic activity as an esterase.8. The method according to claim 7 , wherein placing a polypeptide at least 90% sequence identity to SEQ ID No. 287 in fluid contact with a polysaccharide claim 7 , lignocellulose claim 7 , cellulose claim 7 , hemicellulose claim 7 , lignin claim 7 , starch claim 7 , chitin claim 7 , polyhydroxybutyrate claim 7 , heteroxylans claim 7 , glycoside claim 7 , xylan claim 7 , glucan claim 7 , galactan claim 7 , or mannan decorating group occurs at or below about pH 4.9. The method according to claim 7 , wherein placing a polypeptide having at least 90% sequence identity to SEQ ID No. 287 in fluid contact with a polysaccharide claim 7 , lignocellulose claim 7 , cellulose claim 7 , hemicellulose claim 7 , lignin claim 7 , starch claim 7 , chitin claim 7 , polyhydroxybutyrate claim 7 , heteroxylans claim 7 , glycoside claim 7 , xylan claim 7 , glucan claim 7 , galactan claim 7 ...

Compositions and methods for treating eye infections and disease

The present invention provides compositions and methods for identifying subjects suffering from dry eye that can be treated by topical administration of a composition comprising lacritin or a bioactive fragment thereof. The application discloses in part that a ˜90 KDa deglycanated form of syndecan-1 is abundant in tears of normal individuals but not individuals suffering from dry eye, whereas a ˜25 kDa syndecan-1 fragment is detectable in dry, but not normal tears.

FORMULATION OF GLUCOSINOLATES AND MYROSINASE

Disclosed is a formulation which contains microcapsules which contain a core containing an extract rich in glucosinolates obtained from crucifers and a biopolymer, and an enteric coating containing myrosinase and a biopolymer. Also, disclosed is a procedure for obtaining the same and to a use of the formulation as such, or in dietetic food supplements for humans or animals due to its immunostimulant activity. 1. A formulation which comprises microcapsules which comprise two layers: (i) one core or interior central part comprising an extract rich in glucosinolates and at least one biopolymer being a polysaccharide and (ii) one enteric coating or exterior layer surrounding the core comprising myrosinase and at least one biopolymer.2. The formulation according to claim 1 , wherein the extract rich in glucosinolates is obtained from a crucifer plant.3. The formulation according to claim 2 , wherein the plant is broccoli.4. The formulation according to claim 1 , wherein the polysaccharide of the core is alginate.5. The formulation according to claim 1 , wherein the biopolymer of the coating is selected from the group consisting of (i) chitosan alginate claim 1 , (ii) pectin claim 1 , and (iii) pectin alginate.6. The formulation according to claim 1 , wherein a relation by weight between the extract rich in glucosinolates and myrosinase is such that the quantity of myrosinase is in a relation of between 5-50% by weight with respect to the quantity of glucoraphanin present in the extract used in an internal layer.7. The formulation according to claim 6 , wherein the relation by weight between the extract rich in glucosinolates and myrosinase is such that the quantity of myrosinase is in a relation of between 10-45% by weight with respect to the quantity of glucoraphanin present in the extract used in the core.8. The formulation according to claim 1 , wherein a relation by weight between the biopolymer of the core and the extract is between 0.5%-5% of the biopolymer and 95 ...