Polypeptides Having Cellobiohydrolase I Activity and Polynucleotides Encoding Same
This application is a divisional of U.S. application Ser. No. 13/681,490 filed on Nov. 20, 2012, now allowed, which is a divisional of U.S. application Ser. No. 13/646,980 filed on Oct. 8, 2012, now U.S. Pat. No. 8,507,238, which is a divisional of U.S. application Ser. No. 13/483,389 filed on May 30, 2012, now allowed, which is a divisional of U.S. application Ser. No. 12/818,861 filed on Jun. 18, 2010, now U.S. Pat. No. 8,338,156, which is a continuation of U.S. application Ser. No. 10/481,179 filed Dec. 17, 2003, now U.S. Pat. No. 7,785,853, which is a 35 U.S.C. 371 national application of international application no. PCT/DK02/000429 filed Jun. 26, 2002, which claims priority or the benefit under 35 U.S.C. 119 of Danish application no. PA 2001 01000 filed on Jun. 26, 2001, the contents of which are fully incorporated herein by reference. The present invention relates to polypeptides having cellobiohydrolase I (also referred to as CBH I or CBH 1) activity and polynucleotides having a nucleotide sequence which encodes for the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid constructs as well as methods for producing and using the polypeptides. Cellulose is an important industrial raw material and a source of renewable energy. The physical structure and morphology of native cellulose are complex and the fine details of its structure have been difficult to determine experimentally. However, the chemical composition of cellulose is simple, consisting of D-glucose residues linked by beta-1,4-glycosidic bonds to form linear polymers with chains length of over 10,000 glycosidic residues. In order to be efficient, the digestion of cellulose requires several types of enzymes acting cooperatively. At least three categories of enzymes are necessary to convert cellulose into glucose: endo (1,4)-beta-D-glucanases (EC 3.2.1.4) that cut the cellulose chains at random; cellobiohydrolases (EC 3.2.1.91) which cleave cellobiosyl units from the cellulose chain ends and beta-glucosidases (EC 3.2.1.21) that convert cellobiose and soluble cellodextrins into glucose. Among these three categories of enzymes involved in the biodegradation of cellulose, cellobiohydrolases are the key enzymes for the degradation of native crystalline cellulose. Exo-cellobiohydrolases (Cellobiohydrolase I, or CBH I) refer to the cellobiohydrolases which degrade cellulose by hydrolyzing the cellobiose from the reducing end of the cellulose polymer chains. It is an object of the present invention to provide improved polypeptides having cellobiohydrolase I activity and polynucleotides encoding the polypeptides. The improved polypeptides may have improved specific activity and/or improved stability—in particular improved thermostability. The polypeptides may also have an improved ability to resist inhibition by cellobiose. In a first aspect the present invention relates to a polypeptide having cellobiohydrolase I activity, selected from the group consisting of: (a) a polypeptide comprising an amino acid sequence selected from the group consisting of: an amino acid sequence which has at least 80% identity with amino acids 1 to 526 of SEQ ID NO:2, an amino acid sequence which has at least 80% identity with amino acids 1 to 529 of SEQ ID NO:4, an amino acid sequence which has at least 80% identity with amino acids 1 to 451 of SEQ ID NO:6, an amino acid sequence which has at least 80% identity with amino acids 1 to 457 of SEQ ID NO:8, an amino acid sequence which has at least 80% identity with amino acids 1 to 538 of SEQ ID NO:10, an amino acid sequence which has at least 70% identity with amino acids 1 to 415 of SEQ ID NO:12, an amino acid sequence which has at least 70% identity with amino acids 1 to 447 of SEQ ID NO:14, an amino acid sequence which has at least 80% identity with amino acids 1 to 452 of SEQ ID NO:16, an amino acid sequence which has at least 80% identity with amino acids 1 to 454 of SEQ ID NO:38, an amino acid sequence which has at least 80% identity with amino acids 1 to 458 of SEQ ID NO:40, an amino acid sequence which has at least 80% identity with amino acids 1 to 450 of SEQ ID NO:42, an amino acid sequence which has at least 80% identity with amino acids 1 to 446 of SEQ ID NO:44, an amino acid sequence which has at least 80% identity with amino acids 1 to 527 of SEQ ID NO:46, an amino acid sequence which has at least 80% identity with amino acids 1 to 455 of SEQ ID NO:48, an amino acid sequence which has at least 80% identity with amino acids 1 to 464 of SEQ ID NO:50, an amino acid sequence which has at least 80% identity with amino acids 1 to 460 of SEQ ID NO:52, an amino acid sequence which has at least 80% identity with amino acids 1 to 450 of SEQ ID NO:54, an amino acid sequence which has at least 80% identity with amino acids 1 to 532 of SEQ ID NO:56, an amino acid sequence which has at least 80% identity with amino acids 1 to 460 of SEQ ID NO:58, an amino acid sequence which has at least 80% identity with amino acids 1 to 525 of SEQ ID NO:60, and an amino acid sequence which has at least 80% identity with amino acids 1 to 456 of SEQ ID NO:66; (b) a polypeptide comprising an amino acid sequence selected from the group consisting of: an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 70% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 70% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence which has at least 80% identity with the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in an amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in (c) a polypeptide comprising an amino acid sequence selected from the group consisting of: an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1578 of SEQ ID NO:1, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1587 of SEQ ID NO:3, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1353 of SEQ ID NO:5, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1371 of SEQ ID NO:7, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1614 of SEQ ID NO:9, an amino acid sequence which has at least 70% identity with the polypeptide encoded by nucleotides 1 to 1245 of SEQ ID NO:11, an amino acid sequence which has at least 70% identity with the polypeptide encoded by nucleotides 1 to 1341 of SEQ ID NO:13, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1356 of SEQ ID NO:15, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1365 of SEQ ID NO:37, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1377 of SEQ ID NO:39, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1353 of SEQ ID NO:41, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1341 of SEQ ID NO:43, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1584 of SEQ ID NO:45, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1368 of SEQ ID NO:47, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1395 of SEQ ID NO:49, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1383 of SEQ ID NO:51, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1353 of SEQ ID NO:53, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1599 of SEQ ID NO:55, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1383 of SEQ ID NO:57, an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1578 of SEQ ID NO:59, and an amino acid sequence which has at least 80% identity with the polypeptide encoded by nucleotides 1 to 1371 of SEQ ID NO:65; (d) a polypeptide which is encoded by a nucleotide sequence which hybridizes under high stringency conditions with a polynucleotide probe selected from the group consisting of: (i) the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 1578 of SEQ ID NO:1, nucleotides 1 to 1587 of SEQ ID NO:3, nucleotides 1 to 1353 of SEQ ID NO:5, nucleotides 1 to 1371 of SEQ ID NO:7, nucleotides 1 to 1614 of SEQ ID NO:9, nucleotides 1 to 1245 of SEQ ID NO:11, nucleotides 1 to 1341 of SEQ ID NO:13, nucleotides 1 to 1356 of SEQ ID NO:15, nucleotides 1 to 1365 of SEQ ID NO:37, nucleotides 1 to 1377 of SEQ ID NO:39, nucleotides 1 to 1353 of SEQ ID NO:41, nucleotides 1 to 1341 of SEQ ID NO:43, nucleotides 1 to 1584 of SEQ ID NO:45, nucleotides 1 to 1368 of SEQ ID NO:47, nucleotides 1 to 1395 of SEQ ID NO:49, nucleotides 1 to 1383 of SEQ ID NO:51, nucleotides 1 to 1353 of SEQ ID NO:53, nucleotides 1 to 1599 of SEQ ID NO:55, nucleotides 1 to 1383 of SEQ ID NO:57, nucleotides 1 to 1578 of SEQ ID NO:59, and nucleotides 1 to 1371 of SEQ ID NO:65; (ii) the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 500 of SEQ ID NO:1, nucleotides 1 to 500 of SEQ ID NO:3, nucleotides 1 to 500 of SEQ ID NO:5, nucleotides 1 to 500 of SEQ ID NO:7, nucleotides 1 to 500 of SEQ ID NO:9, nucleotides 1 to 500 of SEQ ID NO:11, nucleotides 1 to 500 of SEQ ID NO:13, nucleotides 1 to 500 of SEQ ID NO:15, nucleotides 1 to 500 of SEQ ID NO:37, nucleotides 1 to 500 of SEQ ID NO:39, nucleotides 1 to 500 of SEQ ID NO:41, nucleotides 1 to 500 of SEQ ID NO:43, nucleotides 1 to 500 of SEQ ID NO:45, nucleotides 1 to 500 of SEQ ID NO:47, nucleotides 1 to 500 of SEQ ID NO:49, nucleotides 1 to 500 of SEQ ID NO:51, nucleotides 1 to 500 of SEQ ID NO:53, nucleotides 1 to 500 of SEQ ID NO:55, nucleotides 1 to 500 of SEQ ID NO:57, nucleotides 1 to 500 of SEQ ID NO:59, nucleotides 1 to 500 of SEQ ID NO:65, nucleotides 1 to 221 of SEQ ID NO:17, nucleotides 1 to 239 of SEQ ID NO:18, nucleotides 1 to 199 of SEQ ID NO:19, nucleotides 1 to 191 of SEQ ID NO:20, nucleotides 1 to 232 of SEQ ID NO:21, nucleotides 1 to 467 of SEQ ID NO:22, nucleotides 1 to 534 of SEQ ID NO:23, nucleotides 1 to 563 of SEQ ID NO:24, nucleotides 1 to 218 of SEQ ID NO:25, nucleotides 1 to 492 of SEQ ID NO:26, nucleotides 1 to 481 of SEQ ID NO:27, nucleotides 1 to 463 of SEQ ID NO:28, nucleotides 1 to 513 of SEQ ID NO:29, nucleotides 1 to 579 of SEQ ID NO:30, nucleotides 1 to 514 of SEQ ID NO:31, nucleotides 1 to 477 of SEQ ID NO:32, nucleotides 1 to 500 of SEQ ID NO:33, nucleotides 1 to 470 of SEQ ID NO:34, nucleotides 1 to 491 of SEQ ID NO:35, nucleotides 1 to 221 of SEQ ID NO:36, nucleotides 1 to 519 of SEQ ID NO:61, nucleotides 1 to 497 of SEQ ID NO:62, nucleotides 1 to 498 of SEQ ID NO:63, nucleotides 1 to 525 of SEQ ID NO:64, and nucleotides 1 to 951 of SEQ ID NO:67; and (iii) the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 200 of SEQ ID NO:1, nucleotides 1 to 200 of SEQ ID NO:3, nucleotides 1 to 200 of SEQ ID NO:5, nucleotides 1 to 200 of SEQ ID NO:7, nucleotides 1 to 200 of SEQ ID NO:9, nucleotides 1 to 200 of SEQ ID NO:11, nucleotides 1 to 200 of SEQ ID NO:13, nucleotides 1 to 200 of SEQ ID NO:15, nucleotides 1 to 200 of SEQ ID NO:37, nucleotides 1 to 200 of SEQ ID NO:39, nucleotides 1 to 200 of SEQ ID NO:41, nucleotides 1 to 200 of SEQ ID NO:43, nucleotides 1 to 200 of SEQ ID NO:45, nucleotides 1 to 200 of SEQ ID NO:47, nucleotides 1 to 200 of SEQ ID NO:49, nucleotides 1 to 200 of SEQ ID NO:51, nucleotides 1 to 200 of SEQ ID NO:53, nucleotides 1 to 200 of SEQ ID NO:55, nucleotides 1 to 200 of SEQ ID NO:57, nucleotides 1 to 200 of SEQ ID NO:59, and nucleotides 1 to 200 of SEQ ID NO:65; and (e) a fragment of (a), (b) or (c) that has cellobiohydrolase I activity. In a second aspect the present invention relates to a polynucleotide having a nucleotide sequence which encodes for the polypeptide of the invention. In a third aspect the present invention relates to a nucleic acid construct comprising the nucleotide sequence, which encodes for the polypeptide of the invention, operably linked to one or more control sequences that direct the production of the polypeptide in a suitable host. In a fourth aspect the present invention relates to a recombinant expression vector comprising the nucleic acid construct of the invention. In a fifth aspect the present invention relates to a recombinant host cell comprising the nucleic acid construct of the invention. In a sixth aspect the present invention relates to a method for producing a polypeptide of the invention, the method comprising: (a) cultivating a strain, which in its wild-type form is capable of producing the polypeptide, to produce the polypeptide; and (b) recovering the polypeptide. In a seventh aspect the present invention relates to a method for producing a polypeptide of the invention, the method comprising: (a) cultivating a recombinant host cell of the invention under conditions conducive for production of the polypeptide; and (b) recovering the polypeptide. In an eight aspect the present invention relates to a method for in-situ production of a polypeptide of the invention, the method comprising: (a) cultivating a recombinant host cell of the invention under conditions conducive for production of the polypeptide; and (b) contacting the polypeptide with a desired substrate without prior recovery of the polypeptide. Other aspects of the present invention will be apparent from the below description and from the appended claims. Prior to discussing the present invention in further details, the following terms and conventions will first be defined: Substantially pure polypeptide: In the present context, the term “substantially pure polypeptide” means a polypeptide preparation which contains at the most 10% by weight of other polypeptide material with which it is natively associated (lower percentages of other polypeptide material are preferred, e.g., at the most 8% by weight, at the most 6% by weight, at the most 5% by weight, at the most 4% at the most 3% by weight, at the most 2% by weight, at the most 1% by weight, and at the most ½% by weight). Thus, it is preferred that the substantially pure polypeptide is at least 92% pure, i.e., that the polypeptide constitutes at least 92% by weight of the total polypeptide material present in the preparation, and higher percentages are preferred such as at least 94% pure, at least 95% pure, at least 96% pure, at least 96% pure, at least 97% pure, at least 98% pure, at least 99%, and at the most 99.5% pure. The polypeptides disclosed herein are preferably in a substantially pure form. In particular, it is preferred that the polypeptides disclosed herein are in “essentially pure form”, i.e., that the polypeptide preparation is essentially free of other polypeptide material with which it is natively associated. This can be accomplished, for example, by preparing the polypeptide by means of well-known recombinant methods. Herein, the term “substantially pure polypeptide” is synonymous with the terms “isolated polypeptide” and “polypeptide in isolated form”. Cellobiohydrolase I activity: The term “cellobiohydrolase I activity” is defined herein as a cellulose 1,4-beta-cellobiosidase (also referred to as Exo-glucanase, Exo-cellobiohydrolase or 1,4-beta-cellobiohydrolase) activity, as defined in the enzyme class EC 3.2.1.91, which catalyzes the hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the reducing ends of the chains. For purposes of the present invention, cellobiohydrolase I activity may be determined according to the procedure described in Example 2. In an embodiment, cellobiohydrolase I activity may be determined according to the procedure described in Deshpande et al., The polypeptides of the present invention should preferably have at least 20% of the cellobiohydrolase I activity of a polypeptide consisting of an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66. In a particular preferred embodiment, the polypeptides should have at least 40%, such as at least 50%, preferably at least 60%, such as at least 70%, more preferably at least 80%, such as at least 90%, most preferably at least 95%, such as about or at least 100% of the cellobiohydrolase I activity of the polypeptide consisting of the amino acid sequence selected from the group consisting of amino acids 1 to 526 of SEQ ID NO:2, amino acids 1 to 529 of SEQ ID NO:4, amino acids 1 to 451 of SEQ ID NO:6, amino acids 1 to 457 of SEQ ID NO:8, amino acids 1 to 538 of SEQ ID NO:10, amino acids 1 to 415 of SEQ ID NO:12, amino acids 1 to 447 of SEQ ID NO:14, amino acids 1 to 452 of SEQ ID NO:16, amino acids 1 to 454 of SEQ ID NO:38, amino acids 1 to 458 of SEQ ID NO:40, amino acids 1 to 450 of SEQ ID NO:42, amino acids 1 to 446 of SEQ ID NO:44, amino acids 1 to 527 of SEQ ID NO:46, amino acids 1 to 455 of SEQ ID NO:48, amino acids 1 to 464 of SEQ ID NO:50, amino acids 1 to 460 of SEQ ID NO:52, amino acids 1 to 450 of SEQ ID NO:54, amino acids 1 to 532 of SEQ ID NO:56, amino acids 1 to 460 of SEQ ID NO:58, amino acids 1 to 525 of SEQ ID NO:60, and amino acids 1 to 456 of SEQ ID NO:66. Identity: In the present context, the homology between two amino acid sequences or between two nucleotide sequences is described by the parameter “identity”. For purposes of the present invention, the degree of identity between two amino acid sequences is determined by using the program FASTA included in version 2.0× of the FASTA program package (see Pearson and Lipman, 1988, “Improved Tools for Biological Sequence Analysis”, PNAS 85:2444-2448; and Pearson, 1990, “Rapid and Sensitive Sequence Comparison with FASTP and FASTA”, The degree of identity between two nucleotide sequences is determined using the same algorithm and software package as described above. The scoring matrix used was the identity matrix, gap penalty was −16, and gap extension penalty was −4. Fragment: When used herein, a “fragment” of a sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66 is a polypeptide having one or more amino acids deleted from the amino and/or carboxyl terminus of this amino acid sequence. Preferably, a fragment is a polypeptide having the amino acid sequence deleted corresponding to the “cellulose-binding domain” and/or the “linker domain” of Allelic variant: In the present context, the term “allelic variant” denotes any of two or more alternative forms of a gene occupying the same chromosomal locus. Allelic variation arises naturally through mutation, and may result in polymorphism within populations. Gene mutations can be silent (no change in the encoded polypeptide) or may encode polypeptides having altered amino acid sequences. An allelic variant of a polypeptide is a polypeptide encoded by an allelic variant of a gene. Substantially pure polynucleotide: The term “substantially pure polynucleotide” as used herein refers to a polynucleotide preparation, wherein the polynucleotide has been removed from its natural genetic milieu, and is thus free of other extraneous or unwanted coding sequences and is in a form suitable for use within genetically engineered protein production systems. Thus, a substantially pure polynucleotide contains at the most 10% by weight of other polynucleotide material with which it is natively associated (lower percentages of other polynucleotide material are preferred, e.g., at the most 8% by weight, at the most 6% by weight, at the most 5% by weight, at the most 4% at the most 3% by weight, at the most 2% by weight, at the most 1% by weight, and at the most ½% by weight). A substantially pure polynucleotide may, however, include naturally occurring 5′ and 3′ untranslated regions, such as promoters and terminators. It is preferred that the substantially pure polynucleotide is at least 92% pure, i.e., that the polynucleotide constitutes at least 92% by weight of the total polynucleotide material present in the preparation, and higher percentages are preferred such as at least 94% pure, at least 95% pure, at least 96% pure, at least 96% pure, at least 97% pure, at least 98% pure, at least 99%, and at the most 99.5% pure. The polynucleotides disclosed herein are preferably in a substantially pure form. In particular, it is preferred that the polynucleotides disclosed herein are in “essentially pure form”, i.e., that the polynucleotide preparation is essentially free of other polynucleotide material with which it is natively associated. Herein, the term “substantially pure polynucleotide” is synonymous with the terms “isolated polynucleotide” and “polynucleotide in isolated form”. Modification(s): In the context of the present invention the term “modification(s)” is intended to mean any chemical modification of a polypeptide consisting of an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66, as well as genetic manipulation of the DNA encoding that polypeptide. The modification(s) can be replacement(s) of the amino acid side chain(s), substitution(s), deletion(s) and/or insertions(s) in or at the amino acid(s) of interest. Artificial variant: When used herein, the term “artificial variant” means a polypeptide having cellobiohydrolase I activity, which has been produced by an organism which is expressing a modified gene as compared to SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, or SEQ ID NO:65. The modified gene, from which said variant is produced when expressed in a suitable host, is obtained through human intervention by modification of a nucleotide sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65. cDNA: The term “cDNA” when used in the present context, is intended to cover a DNA molecule which can be prepared by reverse transcription from a mature, spliced, mRNA molecule derived from a eukaryotic cell. cDNA lacks the intron sequences that are usually present in the corresponding genomic DNA. The initial, primary RNA transcript is a precursor to mRNA and it goes through a series of processing events before appearing as mature spliced mRNA. These events include the removal of intron sequences by a process called splicing. When cDNA is derived from mRNA it therefore lacks intron sequences. Nucleic acid construct: When used herein, the term “nucleic acid construct” means a nucleic acid molecule, either single- or double-stranded, which is isolated from a naturally occurring gene or which has been modified to contain segments of nucleic acids in a manner that would not otherwise exist in nature. The term nucleic acid construct is synonymous with the term “expression cassette” when the nucleic acid construct contains the control sequences required for expression of a coding sequence of the present invention. Control sequence: The term “control sequences” is defined herein to include all components, which are necessary or advantageous for the expression of a polypeptide of the present invention. Each control sequence may be native or foreign to the nucleotide sequence encoding the polypeptide. Such control sequences include, but are not limited to, a leader, polyadenylation sequence, propeptide sequence, promoter, signal peptide sequence, and transcription terminator. At a minimum, the control sequences include a promoter, and transcriptional and translational stop signals. The control sequences may be provided with linkers for the purpose of introducing specific restriction sites facilitating ligation of the control sequences with the coding region of the nucleotide sequence encoding a polypeptide. Operably linked: The term “operably linked” is defined herein as a configuration in which a control sequence is appropriately placed at a position relative to the coding sequence of the DNA sequence such that the control sequence directs the expression of a polypeptide. Coding sequence: When used herein the term “coding sequence” is intended to cover a nucleotide sequence, which directly specifies the amino acid sequence of its protein product. The boundaries of the coding sequence are generally determined by an open reading frame, which usually begins with the ATG start codon. The coding sequence typically include DNA, cDNA, and recombinant nucleotide sequences. Expression: In the present context, the term “expression” includes any step involved in the production of the polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion. Expression vector: In the present context, the term “expression vector” covers a DNA molecule, linear or circular, that comprises a segment encoding a polypeptide of the invention, and which is operably linked to additional segments that provide for its transcription. Host cell: The term “host cell”, as used herein, includes any cell type which is susceptible to transformation with a nucleic acid construct. The terms “polynucleotide probe”, “hybridization” as well as the various stringency conditions are defined in the section entitled “Polypeptides Having Cellobiohydrolase I Activity”. Thermostability: The term “thermostability”, as used herein, is measured as described in Example 2. In a first embodiment, the present invention relates to polypeptides having cellobiohydrolase I activity and where the polypeptides comprises, preferably consists of, an amino acid sequence which has a degree of identity to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66 (i.e., the mature polypeptide) of at least 65%, preferably at least 70%, e.g., at least 75%, more preferably at least 80%, such as at least 85%, even more preferably at least 90%, most preferably at least 95%, e.g., at least 96%, such as at least 97%, and even most preferably at least 98%, such as at least 99% (hereinafter “homologous polypeptides”). In an interesting embodiment, the amino acid sequence differs by at the most ten amino acids (e.g., by ten amino acids), in particular by at the most five amino acids (e.g., by five amino acids), such as by at the most four amino acids (e.g., by four amino acids), e.g., by at the most three amino acids (e.g., by three amino acids) from an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66. In a particular interesting embodiment, the amino acid sequence differs by at the most two amino acids (e.g., by two amino acids), such as by one amino acid from an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66. Preferably, the polypeptides of the present invention comprise an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66; an allelic variant thereof; or a fragment thereof that has cellobiohydrolase I activity. In another preferred embodiment, the polypeptide of the present invention consists of an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66. The polypeptide of the invention may be a wild-type cellobiohydrolase I identified and isolated from a natural source. Such wild-type polypeptides may be specifically screened for by standard techniques known in the art, such as molecular screening as described in Example 1. Furthermore, the polypeptide of the invention may be prepared by the DNA shuffling technique, such as described in Ness et al., Examples of conservative substitutions are within the group of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine, valine and methionine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine and threonine). Amino acid substitutions which do not generally alter the specific activity are known in the art and are described, for example, by H. Neurath and R. L. Hill, 1979, In an interesting embodiment of the invention, the amino acid changes are of such a nature that the physico-chemical properties of the polypeptides are altered. For example, amino acid changes may be performed, which improve the thermal stability of the polypeptide, which alter the substrate specificity, which changes the pH optimum, and the like. Preferably, the number of such substitutions, deletions and/or insertions as compared to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66 is at the most 10, such as at the most 9, e.g., at the most 8, more preferably at the most 7, e.g., at the most 6, such as at the most 5, most preferably at the most 4, e.g., at the most 3, such as at the most 2, in particular at the most 1. The present inventors have isolated nucleotide sequences encoding polypeptides having cellobiohydrolase I activity from the microorganisms selected from the group consisting of Preferably, the polypeptides of the present invention comprise the amino acid sequence of the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence inserted into a plasmid present in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CBS 109513, DSM 14348, CGMCC No. 0580, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. In another preferred embodiment, the polypeptide of the present invention consists of the amino acid sequence of the polypeptide encoded by the cellobiohydrolase I encoding part of the nucleotide sequence inserted into a plasmid present in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CBS 109513, DSM 14348, and CGMCC No. 0580, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. In a similar way as described above, the polypeptide of the invention may be an artificial variant which comprises, preferably consists of, an amino acid sequence that has at least one substitution, deletion and/or insertion of an amino acid as compared to the amino acid sequence encoded by the cellobiohydrolase I encoding part of the nucleotide sequence inserted into a plasmid present in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CBS 109513, DSM 14348, and CGMCC No. 0580, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. In a third embodiment, the present invention relates to polypeptides having cellobiohydrolase I activity which are encoded by nucleotide sequences which hybridize under very low stringency conditions, preferably under low stringency conditions, more preferably under medium stringency conditions, more preferably under medium-high stringency conditions, even more preferably under high stringency conditions, and most preferably under very high stringency conditions with a polynucleotide probe selected from the group consisting of (i) the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 1578 of SEQ ID NO:1, nucleotides 1 to 1587 of SEQ ID NO:3, nucleotides 1 to 1353 of SEQ ID NO:5, nucleotides 1 to 1371 of SEQ ID NO:7, nucleotides 1 to 1614 of SEQ ID NO:9, nucleotides 1 to 1245 of SEQ ID NO:11, nucleotides 1 to 1341 of SEQ ID NO:13, nucleotides 1 to 1356 of SEQ ID NO:15, nucleotides 1 to 1365 of SEQ ID NO:37, nucleotides 1 to 1377 of SEQ ID NO:39, nucleotides 1 to 1353 of SEQ ID NO:41, nucleotides 1 to 1341 of SEQ ID NO:43, nucleotides 1 to 1584 of SEQ ID NO:45, nucleotides 1 to 1368 of SEQ ID NO:47, nucleotides 1 to 1395 of SEQ ID NO:49, nucleotides 1 to 1383 of SEQ ID NO:51, nucleotides 1 to 1353 of SEQ ID NO:53, nucleotides 1 to 1599 of SEQ ID NO:55, nucleotides 1 to 1383 of SEQ ID NO:57, nucleotides 1 to 1578 of SEQ ID NO:59, and nucleotides 1 to 1371 of SEQ ID NO:65; (ii) the complementary strand of the nucleotides selected from the group consisting of nucleotides 1 to 500 of SEQ ID NO:1, nucleotides 1 to 500 of SEQ ID NO:3, nucleotides 1 to 500 of SEQ ID NO:5, nucleotides 1 to 500 of SEQ ID NO:7, nucleotides 1 to 500 of SEQ ID NO:9, nucleotides 1 to 500 of SEQ ID NO:11, nucleotides 1 to 500 of SEQ ID NO:13, nucleotides 1 to 500 of SEQ ID NO:15, nucleotides 1 to 500 of SEQ ID NO:37, nucleotides 1 to 500 of SEQ ID NO:39, nucleotides 1 to 500 of SEQ ID NO:41, nucleotides 1 to 500 of SEQ ID NO:43, nucleotides 1 to 500 of SEQ ID NO:45, nucleotides 1 to 500 of SEQ ID NO:47, nucleotides 1 to 500 of SEQ ID NO:49, nucleotides 1 to 500 of SEQ ID NO:51, nucleotides 1 to 500 of SEQ ID NO:53, nucleotides 1 to 500 of SEQ ID NO:55, nucleotides 1 to 500 of SEQ ID NO:57, nucleotides 1 to 500 of SEQ ID NO:59, nucleotides 1 to 500 of SEQ ID NO:65, nucleotides 1 to 221 of SEQ ID NO:17, nucleotides 1 to 239 of SEQ ID NO:18, nucleotides 1 to 199 of SEQ ID NO:19, nucleotides 1 to 191 of SEQ ID NO:20, nucleotides 1 to 232 of SEQ ID NO:21, nucleotides 1 to 467 of SEQ ID NO:22, nucleotides 1 to 534 of SEQ ID NO:23, nucleotides 1 to 563 of SEQ ID NO:24, nucleotides 1 to 218 of SEQ ID NO:25, nucleotides 1 to 492 of SEQ ID NO:26, nucleotides 1 to 481 of SEQ ID NO:27, nucleotides 1 to 463 of SEQ ID NO:28, nucleotides 1 to 513 of SEQ ID NO:29, nucleotides 1 to 579 of SEQ ID NO:30, nucleotides 1 to 514 of SEQ ID NO:31, nucleotides 1 to 477 of SEQ ID NO:32, nucleotides 1 to 500 of SEQ ID NO:33, nucleotides 1 to 470 of SEQ ID NO:34, nucleotides 1 to 491 of SEQ ID NO:35, nucleotides 1 to 221 of SEQ ID NO:36, nucleotides 1 to 519 of SEQ ID NO:61, nucleotides 1 to 497 of SEQ ID NO:62, nucleotides 1 to 498 of SEQ ID NO:63, nucleotides 1 to 525 of SEQ ID NO:64, and nucleotides 1 to 951 of SEQ ID NO:67; and (iii) the complementary strand of the nucleotides selected from the group consisting of nucleotides 1 to 200 of SEQ ID NO:1, nucleotides 1 to 200 of SEQ ID NO:3, nucleotides 1 to 200 of SEQ ID NO:5, nucleotides 1 to 200 of SEQ ID NO:7, nucleotides 1 to 200 of SEQ ID NO:9, nucleotides 1 to 200 of SEQ ID NO:11, nucleotides 1 to 200 of SEQ ID NO:13, nucleotides 1 to 200 of SEQ ID NO:15, nucleotides 1 to 200 of SEQ ID NO:37, nucleotides 1 to 200 of SEQ ID NO:39, nucleotides 1 to 200 of SEQ ID NO:41, nucleotides 1 to 200 of SEQ ID NO:43, nucleotides 1 to 200 of SEQ ID NO:45, nucleotides 1 to 200 of SEQ ID NO:47, nucleotides 1 to 200 of SEQ ID NO:49, nucleotides 1 to 200 of SEQ ID NO:51, nucleotides 1 to 200 of SEQ ID NO:53, nucleotides 1 to 200 of SEQ ID NO:55, nucleotides 1 to 200 of SEQ ID NO:57, nucleotides 1 to 200 of SEQ ID NO:59, and nucleotides 1 to 200 of SEQ ID NO:65 (Sambrook et al., 1989, In another embodiment, the present invention relates to polypeptides having cellobiohydrolase I activity which are encoded by the cellobiohydrolase I encoding part of the nucleotide sequence present in a microorganism selected from the group consisting of: a microorganism belonging to Zygomycota, preferably belonging to the Mucorales, more preferably belonging to the family Mucoraceae, most preferably belonging to the genus a microorganism belonging to the Oomycetes, preferably to the order Pythiales, more preferably to the family Pythiaceae, most preferably to the genus a microorganism belonging to Auriculariales (an order of the Basidiomycota, Hymenomycetes), preferably belonging to the family Exidiaceae, more preferably belonging to the genus a microorganism belonging to Xylariales (an order of the Ascomycota, Sordariomycetes), preferably belonging to the family Xylariaceae, more preferably belonging to the genus a microorganism belonging to Dothideales (an order of the Ascomycota, Dothideomycetes), preferably belonging to the family Dothideaceae, more preferably belonging to the genus a microorganism belonging to Pezizales (an order of the Ascomycota), preferably belonging to the family Pyronemataceae, more preferably belonging to the genus a microorganism belonging to the family Rigidiporaceae (under Basidiomycota, Hymenomycetes, Hymenomycetales), more preferably belonging to the genus a microorganism belonging to the family Meruliaceae (under Basidiomycota, Hymenomycetes, Sterealesales), more preferably belonging to the genus a microorganism belonging to the family Agaricaceae (under Basidiomycota, Hymenomycetes, Agaricales), more preferably belonging to the genus a microorganism belonging to the family Hypocreaceae (under Ascomycota, Sordariomycetes, Hypocreales), more preferably belonging to the genus a microorganism belonging to the genus a microorganism belonging to the genus a microorganism belonging to the genus a microorganism belonging to the genus a microorganism belonging to the genus a microorganism belonging to the genus a microorganism belonging to the genus a microorganism belonging to the species A nucleotide sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:65, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:19, SEQ ID NO:20, SEQ ID NO:21, SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, SEQ ID NO:25, SEQ ID NO:26, SEQ ID NO:27, SEQ ID NO:28, SEQ ID NO:29, SEQ ID NO:30, SEQ ID NO:31, SEQ ID NO:32, SEQ ID NO:33, SEQ ID NO:34, SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:61, SEQ ID NO:62, SEQ ID NO:63, SEQ ID NO:64, and SEQ ID NO:67, or a subsequence thereof, as well as an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66, or a fragment thereof, may be used to design a polynucleotide probe to identify and clone DNA encoding polypeptides having cellobiohydrolase I activity from strains of different genera or species according to methods well known in the art. In particular, such probes can be used for hybridization with the genomic or cDNA of the genus or species of interest, following standard Southern blotting procedures, in order to identify and isolate the corresponding gene therein. Such probes can be considerably shorter than the entire sequence, but should be at least 15, preferably at least 25, more preferably at least 35 nucleotides in length, such as at least 70 nucleotides in length. It is, however, preferred that the polynucleotide probe is at least 100 nucleotides in length. For example, the polynucleotide probe may be at least 200 nucleotides in length, at least 300 nucleotides in length, at least 400 nucleotides in length or at least 500 nucleotides in length. Even longer probes may be used, e.g., polynucleotide probes which are at least 600 nucleotides in length, at least 700 nucleotides in length, at least 800 nucleotides in length, or at least 900 nucleotides in length. Both DNA and RNA probes can be used. The probes are typically labeled for detecting the corresponding gene (for example, with32P,3H,35S, biotin, or avidin). Thus, a genomic DNA or cDNA library prepared from such other organisms may be screened for DNA which hybridizes with the probes described above and which encodes a polypeptide having cellobiohydrolase I activity. Genomic or other DNA from such other organisms may be separated by agarose or polyacrylamide gel electrophoresis, or other separation techniques. DNA from the libraries or the separated DNA may be transferred to, and immobilized, on nitrocellulose or other suitable carrier materials. In order to identify a clone or DNA which is homologous with SEQ ID NO:1 the carrier material with the immobilized DNA is used in a Southern blot. For purposes of the present invention, hybridization indicates that the nucleotide sequence hybridizes to a labeled polynucleotide probe which hybridizes to the nucleotide sequence shown in SEQ ID NO:1 under very low to very high stringency conditions. Molecules to which the polynucleotide probe hybridizes under these conditions may be detected using X-ray film or by any other method known in the art. Whenever the term “polynucleotide probe” is used in the present context, it is to be understood that such a probe contains at least 15 nucleotides. In an interesting embodiment, the polynucleotide probe is the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 1578 of SEQ ID NO:1, nucleotides 1 to 1302 of SEQ ID NO:1, nucleotides 1 to 1587 of SEQ ID NO:3, nucleotides 1 to 1302 of SEQ ID NO:3, nucleotides 1 to 1353 of SEQ ID NO:5, nucleotides 1 to 1302 of SEQ ID NO:5, nucleotides 1 to 1371 of SEQ ID NO:7, nucleotides 1 to 1302 of SEQ ID NO:7, nucleotides 1 to 1614 of SEQ ID NO:9, nucleotides 1 to 1302 of SEQ ID NO:9, nucleotides 1 to 1245 of SEQ ID NO:11, nucleotides 1 to 1341 of SEQ ID NO:13, nucleotides 1 to 1302 of SEQ ID NO:13, nucleotides 1 to 1356 of SEQ ID NO:15, nucleotides 1 to 1302 of SEQ ID NO:15, nucleotides 1 to 1365 of SEQ ID NO:37, nucleotides 1 to 1302 of SEQ ID NO:37, nucleotides 1 to 1377 of SEQ ID NO:39, nucleotides 1 to 1302 of SEQ ID NO:39, nucleotides 1 to 1353 of SEQ ID NO:41, nucleotides 1 to 1302 of SEQ ID NO:41, nucleotides 1 to 1341 of SEQ ID NO:43, nucleotides 1 to 1302 of SEQ ID NO:43, nucleotides 1 to 1584 of SEQ ID NO:45, nucleotides 1 to 1302 of SEQ ID NO:45, nucleotides 1 to 1368 of SEQ ID NO:47, nucleotides 1 to 1302 of SEQ ID NO:47, nucleotides 1 to 1395 of SEQ ID NO:49, nucleotides 1 to 1302 of SEQ ID NO:49, nucleotides 1 to 1383 of SEQ ID NO:51, nucleotides 1 to 1302 of SEQ ID NO:51, nucleotides 1 to 1353 of SEQ ID NO:53, nucleotides 1 to 1302 of SEQ ID NO:53, nucleotides 1 to 1599 of SEQ ID NO:55, nucleotides 1 to 1302 of SEQ ID NO:55, nucleotides 1 to 1383 of SEQ ID NO:57, nucleotides 1 to 1302 of SEQ ID NO:57, nucleotides 1 to 1578 of SEQ ID NO:59, nucleotides 1 to 1302 of SEQ ID NO:59, nucleotides 1 to 1371 of SEQ ID NO:65, and nucleotides 1 to 1302 of SEQ ID NO:65; or the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 500 of SEQ ID NO:1, nucleotides 1 to 500 of SEQ ID NO:3, nucleotides 1 to 500 of SEQ ID NO:5, nucleotides 1 to 500 of SEQ ID NO:7, nucleotides 1 to 500 of SEQ ID NO:9, nucleotides 1 to 500 of SEQ ID NO:11, nucleotides 1 to 500 of SEQ ID NO:13, nucleotides 1 to 500 of SEQ ID NO:15, nucleotides 1 to 500 of SEQ ID NO:37, nucleotides 1 to 500 of SEQ ID NO:39, nucleotides 1 to 500 of SEQ ID NO:41, nucleotides 1 to 500 of SEQ ID NO:43, nucleotides 1 to 500 of SEQ ID NO:45, nucleotides 1 to 500 of SEQ ID NO:47, nucleotides 1 to 500 of SEQ ID NO:49, nucleotides 1 to 500 of SEQ ID NO:51, nucleotides 1 to 500 of SEQ ID NO:53, nucleotides 1 to 500 of SEQ ID NO:55, nucleotides 1 to 500 of SEQ ID NO:57, nucleotides 1 to 500 of SEQ ID NO:59, nucleotides 1 to 500 of SEQ ID NO:65, nucleotides 1 to 221 of SEQ ID NO:17, nucleotides 1 to 239 of SEQ ID NO:18, nucleotides 1 to 199 of SEQ ID NO:19, nucleotides 1 to 191 of SEQ ID NO:20, nucleotides 1 to 232 of SEQ ID NO:21, nucleotides 1 to 467 of SEQ ID NO:22, nucleotides 1 to 534 of SEQ ID NO:23, nucleotides 1 to 563 of SEQ ID NO:24, nucleotides 1 to 218 of SEQ ID NO:25, nucleotides 1 to 492 of SEQ ID NO:26, nucleotides 1 to 481 of SEQ ID NO:27, nucleotides 1 to 463 of SEQ ID NO:28, nucleotides 1 to 513 of SEQ ID NO:29, nucleotides 1 to 579 of SEQ ID NO:30, nucleotides 1 to 514 of SEQ ID NO:31, nucleotides 1 to 477 of SEQ ID NO:32, nucleotides 1 to 500 of SEQ ID NO:33, nucleotides 1 to 470 of SEQ ID NO:34, nucleotides 1 to 491 of SEQ ID NO:35, nucleotides 1 to 221 of SEQ ID NO:36, nucleotides 1 to 519 of SEQ ID NO:61, nucleotides 1 to 497 of SEQ ID NO:62, nucleotides 1 to 498 of SEQ ID NO:63, nucleotides 1 to 525 of SEQ ID NO:64, and nucleotides 1 to 951 of SEQ ID NO:67; or the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 200 of SEQ ID NO:1, nucleotides 1 to 200 of SEQ ID NO:3, nucleotides 1 to 200 of SEQ ID NO:5, nucleotides 1 to 200 of SEQ ID NO:7, nucleotides 1 to 200 of SEQ ID NO:9, nucleotides 1 to 200 of SEQ ID NO:11, nucleotides 1 to 200 of SEQ ID NO:13, nucleotides 1 to 200 of SEQ ID NO:15, nucleotides 1 to 200 of SEQ ID NO:37, nucleotides 1 to 200 of SEQ ID NO:39, nucleotides 1 to 200 of SEQ ID NO:41, nucleotides 1 to 200 of SEQ ID NO:43, nucleotides 1 to 200 of SEQ ID NO:45, nucleotides 1 to 200 of SEQ ID NO:47, nucleotides 1 to 200 of SEQ ID NO:49, nucleotides 1 to 200 of SEQ ID NO:51, nucleotides 1 to 200 of SEQ ID NO:53, nucleotides 1 to 200 of SEQ ID NO:55, nucleotides 1 to 200 of SEQ ID NO:57, nucleotides 1 to 200 of SEQ ID NO:59, nucleotides 1 to 200 of SEQ ID NO:65, nucleotides 1 to 200 of SEQ ID NO:22, nucleotides 1 to 200 of SEQ ID NO:23, nucleotides 1 to 200 of SEQ ID NO:24, nucleotides 1 to 200 of SEQ ID NO:26, nucleotides 1 to 200 of SEQ ID NO:27, nucleotides 1 to 200 of SEQ ID NO:28, nucleotides 1 to 200 of SEQ ID NO:29, nucleotides 1 to 200 of SEQ ID NO:30, nucleotides 1 to 200 of SEQ ID NO:31, nucleotides 1 to 200 of SEQ ID NO:32, nucleotides 1 to 200 of SEQ ID NO:33, nucleotides 1 to 200 of SEQ ID NO:34, nucleotides 1 to 200 of SEQ ID NO:35, nucleotides 1 to 200 of SEQ ID NO:61, nucleotides 1 to 200 of SEQ ID NO:62, nucleotides 1 to 200 of SEQ ID NO:63, nucleotides 1 to 200 of SEQ ID NO:64, and nucleotides 1 to 200 of SEQ ID NO:67. In another interesting embodiment, the polynucleotide probe is the complementary strand of the nucleotide sequence which encodes a polypeptide selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66. In a further interesting embodiment, the polynucleotide probe is the complementary strand of a nucleotide sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65. In another interesting embodiment, the polynucleotide probe is the complementary strand of the nucleotide sequence contained in a plasmid which is contained in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CGMCC No. 0580, CBS 109513, DSM 14348, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. For long probes of at least 100 nucleotides in length, very low to very high stringency conditions are defined as prehybridization and hybridization at 42° C. in 5×SSPE, 1.0% SDS, 5×Denhardt's solution, 100 micrograms/ml sheared and denatured salmon sperm DNA, following standard Southern blotting procedures. Preferably, the long probes of at least 100 nucleotides do not contain more than 1000 nucleotides. For long probes of at least 100 nucleotides in length, the carrier material is finally washed three times each for 15 minutes using 2×SSC, 0.1% SDS at 42° C. (very low stringency), preferably washed three times each for 15 minutes using 0.5×SSC, 0.1% SDS at 42° C. (low stringency), more preferably washed three times each for 15 minutes using 0.2×SSC, 0.1% SDS at 42° C. (medium stringency), even more preferably washed three times each for 15 minutes using 0.2×SSC, 0.1% SDS at 55° C. (medium-high stringency), most preferably washed three times each for 15 minutes using 0.1×SSC, 0.1% SDS at 60° C. (high stringency), in particular washed three times each for 15 minutes using 0.1×SSC, 0.1% SDS at 68° C. (very high stringency). Although not particularly preferred, it is contemplated that shorter probes, e.g., probes which are from about 15 to 99 nucleotides in length, such as from about 15 to about 70 nucleotides in length, may be also be used. For such short probes, stringency conditions are defined as prehybridization, hybridization, and washing post-hybridization at 5° C. to 10° C. below the calculated Tmusing the calculation according to Bolton and McCarthy (1962, For short probes which are about 15 nucleotides to 99 nucleotides in length, the carrier material is washed once in 6×SCC plus 0.1% SDS for 15 minutes and twice each for 15 minutes using 6×SSC at 5° C. to 10° C. below the calculated Tm. A polypeptide of the present invention may be obtained from microorganisms of any genus. For purposes of the present invention, the term “obtained from” as used herein shall mean that the polypeptide encoded by the nucleotide sequence is produced by a cell in which the nucleotide sequence is naturally present or into which the nucleotide sequence has been inserted. In a preferred embodiment, the polypeptide is secreted extracellularly. A polypeptide of the present invention may be a bacterial polypeptide. For example, the polypeptide may be a gram positive bacterial polypeptide such as a A polypeptide of the present invention may be a fungal polypeptide, and more preferably a yeast polypeptide such as a In an interesting embodiment, the polypeptide is a In another interesting embodiment, the polypeptide is an In a preferred embodiment, the polypeptide is a In a more preferred embodiment, the polypeptide is a It will be understood that for the aforementioned species, the invention encompasses both the perfect and imperfect states, and other taxonomic equivalents, e.g., anamorphs, regardless of the species name by which they are known. Those skilled in the art will readily recognize the identity of appropriate equivalents. Strains of these species are readily accessible to the public in a number of culture collections, such as the American Type Culture Collection (ATCC), Deutsche Sammlung von Mikroorganismen and Zellkulturen GmbH (DSMZ), China General Microbiological Culture Collection Center (CGMCC), Centraalbureau Voor Schimmelcultures (CBS), and Agricultural Research Service Patent Culture Collection, Northern Regional Research Center (NRRL). Furthermore, such polypeptides may be identified and obtained from other sources including microorganisms isolated from nature (e.g., soil, water, plants, animals, etc.) using the above-mentioned probes. Techniques for isolating microorganisms from natural habitats are well known in the art. The nucleotide sequence may then be derived by similarly screening a genomic or cDNA library of another microorganism. Once a nucleotide sequence encoding a polypeptide has been detected with the probe(s), the sequence may be isolated or cloned by utilizing techniques which are known to those of ordinary skill in the art (see, e.g., Sambrook et al., 1989, supra). Polypeptides encoded by nucleotide sequences of the present invention also include fused polypeptides or cleavable fusion polypeptides in which another polypeptide is fused at the N-terminus or the C-terminus of the polypeptide or fragment thereof. A fused polypeptide is produced by fusing a nucleotide sequence (or a portion thereof) encoding another polypeptide to a nucleotide sequence (or a portion thereof) of the present invention. Techniques for producing fusion polypeptides are known in the art, and include ligating the coding sequences encoding the polypeptides so that they are in frame and that expression of the fused polypeptide is under control of the same promoter(s) and terminator. The present invention also relates to polynucleotides having a nucleotide sequence which encodes for a polypeptide of the invention. In particular, the present invention relates to polynucleotides consisting of a nucleotide sequence which encodes for a polypeptide of the invention. In a preferred embodiment, the nucleotide sequence is selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65. In a more preferred embodiment, the nucleotide sequence is the mature polypeptide coding region contained in a plasmid which is contained in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CGMCC No. 0580, CBS 109513, DSM 14348, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. The present invention also encompasses polynucleotides comprising, preferably consisting of, nucleotide sequences which encode a polypeptide consisting of an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66, which differ from a nucleotide sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65 by virtue of the degeneracy of the genetic code. The present invention also relates to polynucleotides comprising, preferably consisting of, a subsequence of a nucleotide sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65 which encode fragments of an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66 that have cellobiohydrolase I activity. A subsequence of a nucleotide sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65 is a nucleotide sequence encompassed by a sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65 except that one or more nucleotides from the 5′ and/or 3′ end have been deleted. The present invention also relates to polynucleotides having, preferably consisting of, a modified nucleotide sequence which comprises at least one modification in the mature polypeptide coding sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, and SEQ ID NO:65, and where the modified nucleotide sequence encodes a polypeptide which consists of an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66. The techniques used to isolate or clone a nucleotide sequence encoding a polypeptide are known in the art and include isolation from genomic DNA, preparation from cDNA, or a combination thereof. The cloning of the nucleotide sequences of the present invention from such genomic DNA can be effected, e.g., by using the well known polymerase chain reaction (PCR) or antibody screening of expression libraries to detect cloned DNA fragments with shared structural features. See, e.g., Innis et al., 1990, The nucleotide sequence may be obtained by standard cloning procedures used in genetic engineering to relocate the nucleotide sequence from its natural location to a different site where it will be reproduced. The cloning procedures may involve excision and isolation of a desired fragment comprising the nucleotide sequence encoding the polypeptide, insertion of the fragment into a vector molecule, and incorporation of the recombinant vector into a host cell where multiple copies or clones of the nucleotide sequence will be replicated. The nucleotide sequence may be of genomic, cDNA, RNA, semisynthetic, synthetic origin, or any combinations thereof. The present invention also relates to a polynucleotide comprising, preferably consisting of, a nucleotide sequence which has a degree of identity with a nucleotide sequence selected from the group consisting of nucleotides 1 to 1578 of SEQ ID NO:1, nucleotides 1 to 1587 of SEQ ID NO:3, nucleotides 1 to 1353 of SEQ ID NO:5, nucleotides 1 to 1371 of SEQ ID NO:7, nucleotides 1 to 1614 of SEQ ID NO:9, nucleotides 1 to 1245 of SEQ ID NO:11, nucleotides 1 to 1341 of SEQ ID NO:13, nucleotides 1 to 1356 of SEQ ID NO:15, nucleotides 1 to 1365 of SEQ ID NO:37, nucleotides 1 to 1377 of SEQ ID NO:39, nucleotides 1 to 1353 of SEQ ID NO:41, nucleotides 1 to 1341 of SEQ ID NO:43, nucleotides 1 to 1584 of SEQ ID NO:45, nucleotides 1 to 1368 of SEQ ID NO:47, nucleotides 1 to 1395 of SEQ ID NO:49, nucleotides 1 to 1383 of SEQ ID NO:51, nucleotides 1 to 1353 of SEQ ID NO:53, nucleotides 1 to 1599 of SEQ ID NO:55, nucleotides 1 to 1383 of SEQ ID NO:57, nucleotides 1 to 1578 of SEQ ID NO:59, nucleotides 1 to 1371 of SEQ ID NO:65, nucleotides 1 to 500 of SEQ ID NO:1, nucleotides 1 to 500 of SEQ ID NO:3, nucleotides 1 to 500 of SEQ ID NO:5, nucleotides 1 to 500 of SEQ ID NO:7, nucleotides 1 to 500 of SEQ ID NO:9, nucleotides 1 to 500 of SEQ ID NO:11, nucleotides 1 to 500 of SEQ ID NO:13, nucleotides 1 to 500 of SEQ ID NO:15, nucleotides 1 to 500 of SEQ ID NO:37, nucleotides 1 to 500 of SEQ ID NO:39, nucleotides 1 to 500 of SEQ ID NO:41, nucleotides 1 to 500 of SEQ ID NO:43, nucleotides 1 to 500 of SEQ ID NO:45, nucleotides 1 to 500 of SEQ ID NO:47, nucleotides 1 to 500 of SEQ ID NO:49, nucleotides 1 to 500 of SEQ ID NO:51, nucleotides 1 to 500 of SEQ ID NO:53, nucleotides 1 to 500 of SEQ ID NO:55, nucleotides 1 to 500 of SEQ ID NO:57, nucleotides 1 to 500 of SEQ ID NO:59, nucleotides 1 to 500 of SEQ ID NO:65, nucleotides 1 to 221 of SEQ ID NO:17, nucleotides 1 to 239 of SEQ ID NO:18, nucleotides 1 to 199 of SEQ ID NO:19, nucleotides 1 to 191 of SEQ ID NO:20, nucleotides 1 to 232 of SEQ ID NO:21, nucleotides 1 to 467 of SEQ ID NO:22, nucleotides 1 to 534 of SEQ ID NO:23, nucleotides 1 to 563 of SEQ ID NO:24, nucleotides 1 to 218 of SEQ ID NO:25, nucleotides 1 to 492 of SEQ ID NO:26, nucleotides 1 to 481 of SEQ ID NO:27, nucleotides 1 to 463 of SEQ ID NO:28, nucleotides 1 to 513 of SEQ ID NO:29, nucleotides 1 to 579 of SEQ ID NO:30, nucleotides 1 to 514 of SEQ ID NO:31, nucleotides 1 to 477 of SEQ ID NO:32, nucleotides 1 to 500 of SEQ ID NO:33, nucleotides 1 to 470 of SEQ ID NO:34, nucleotides 1 to 491 of SEQ ID NO:35, nucleotides 1 to 221 of SEQ ID NO:36, nucleotides 1 to 519 of SEQ ID NO:61, nucleotides 1 to 497 of SEQ ID NO:62, nucleotides 1 to 498 of SEQ ID NO:63, nucleotides 1 to 525 of SEQ ID NO:64, and nucleotides 1 to 951 of SEQ ID NO:67 of at least 70% identity, such as at least 75% identity; preferably, the nucleotide sequence has at least 80% identity, e.g., at least 85% identity, such as at least 90% identity, more preferably at least 95% identity, such as at least 96% identity, e.g., at least 97% identity, even more preferably at least 98% identity, such as at least 99%. Preferably, the nucleotide sequence encodes a polypeptide having cellobiohydrolase I activity. The degree of identity between two nucleotide sequences is determined as described previously (see the section entitled “Definitions”). In another interesting aspect, the present invention relates to a polynucleotide having, preferably consisting of, a nucleotide sequence which has at least 65% identity with the cellobiohydrolase I encoding part of the nucleotide sequence inserted into a plasmid present in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CGMCC No. 0580, CBS 109513, DSM 14348, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. In a preferred embodiment, the degree of identity with the cellobiohydrolase I encoding part of the nucleotide sequence inserted into a plasmid present in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CGMCC No. 0580, CBS 109513, DSM 14348, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750 is at least 70%, e.g., at least 80%, such as at least 90%, more preferably at least 95%, such as at least 96%, e.g., at least 97%, even more preferably at least 98%, such as at least 99%. Preferably, the nucleotide sequence comprises the cellobiohydrolase I encoding part of the nucleotide sequence inserted into a plasmid present in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CGMCC No. 0580, CBS 109513, DSM 14348, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. In an even more preferred embodiment, the nucleotide sequence consists of the cellobiohydrolase I encoding part of the nucleotide sequence inserted into a plasmid present in a deposited microorganism selected from the group consisting of CGMCC No. 0584, CGMCC No. 0581, CGMCC No. 0585, CGMCC No. 0582, CGMCC No. 0583, CGMCC No. 0580, CBS 109513, DSM 14348, DSM 15064, DSM 15065, DSM 15066, DSM 15067, CGMCC No. 0747, CGMCC No. 0748, CGMCC No. 0749, and CGMCC No. 0750. Modification of a nucleotide sequence encoding a polypeptide of the present invention may be necessary for the synthesis of a polypeptide, which comprises an amino acid sequence that has at least one substitution, deletion and/or insertion as compared to an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, and SEQ ID NO:66. These artificial variants may differ in some engineered way from the polypeptide isolated from its native source, e.g., variants that differ in specific activity, thermostability, pH optimum, or the like. It will be apparent to those skilled in the art that such modifications can be made outside the regions critical to the function of the molecule and still result in an active polypeptide. Amino acid residues essential to the activity of the polypeptide encoded by the nucleotide sequence of the invention, and therefore preferably not subject to modification, such as substitution, may be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (see, e.g., Cunningham and Wells, 1989, Moreover, a nucleotide sequence encoding a polypeptide of the present invention may be modified by introduction of nucleotide substitutions which do not give rise to another amino acid sequence of the polypeptide encoded by the nucleotide sequence, but which correspond to the codon usage of the host organism intended for production of the enzyme. The introduction of a mutation into the nucleotide sequence to exchange one nucleotide for another nucleotide may be accomplished by site-directed mutagenesis using any of the methods known in the art. Particularly useful is the procedure, which utilizes a supercoiled, double stranded DNA vector with an insert of interest and two synthetic primers containing the desired mutation. The oligonucleotide primers, each complementary to opposite strands of the vector, extend during temperature cycling by means of Pfu DNA polymerase. On incorporation of the primers, a mutated plasmid containing staggered nicks is generated. Following temperature cycling, the product is treated with DpnI which is specific for methylated and hemimethylated DNA to digest the parental DNA template and to select for mutation-containing synthesized DNA. Other procedures known in the art may also be used. For a general description of nucleotide substitution, see, e.g., Ford et al., 1991, The present invention also relates to a polynucleotide comprising, preferably consisting of, a nucleotide sequence which encodes a polypeptide having cellobiohydrolase I activity, and which hybridizes under very low stringency conditions, preferably under low stringency conditions, more preferably under medium stringency conditions, more preferably under medium-high stringency conditions, even more preferably under high stringency conditions, and most preferably under very high stringency conditions with a polynucleotide probe selected from the group consisting of (i) the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 1578 of SEQ ID NO:1, nucleotides 1 to 1302 of SEQ ID NO:1, nucleotides 1 to 1587 of SEQ ID NO:3, nucleotides 1 to 1302 of SEQ ID NO:3, nucleotides 1 to 1353 of SEQ ID NO:5, nucleotides 1 to 1302 of SEQ ID NO:5, nucleotides 1 to 1371 of SEQ ID NO:7, nucleotides 1 to 1302 of SEQ ID NO:7, nucleotides 1 to 1614 of SEQ ID NO:9, nucleotides 1 to 1302 of SEQ ID NO:9, nucleotides 1 to 1245 of SEQ ID NO:11, nucleotides 1 to 1341 of SEQ ID NO:13, nucleotides 1 to 1302 of SEQ ID NO:13, nucleotides 1 to 1356 of SEQ ID NO:15, nucleotides 1 to 1302 of SEQ ID NO:15, nucleotides 1 to 1365 of SEQ ID NO:37, nucleotides 1 to 1302 of SEQ ID NO:37, nucleotides 1 to 1377 of SEQ ID NO:39, nucleotides 1 to 1302 of SEQ ID NO:39, nucleotides 1 to 1353 of SEQ ID NO:41, nucleotides 1 to 1302 of SEQ ID NO:41, nucleotides 1 to 1341 of SEQ ID NO:43, nucleotides 1 to 1302 of SEQ ID NO:43, nucleotides 1 to 1584 of SEQ ID NO:45, nucleotides 1 to 1302 of SEQ ID NO:45, nucleotides 1 to 1368 of SEQ ID NO:47, nucleotides 1 to 1302 of SEQ ID NO:47, nucleotides 1 to 1395 of SEQ ID NO:49, nucleotides 1 to 1302 of SEQ ID NO:49, nucleotides 1 to 1383 of SEQ ID NO:51, nucleotides 1 to 1302 of SEQ ID NO:51, nucleotides 1 to 1353 of SEQ ID NO:53, nucleotides 1 to 1302 of SEQ ID NO:53, nucleotides 1 to 1599 of SEQ ID NO:55, nucleotides 1 to 1302 of SEQ ID NO:55, nucleotides 1 to 1383 of SEQ ID NO:57, nucleotides 1 to 1302 of SEQ ID NO:57, nucleotides 1 to 1578 of SEQ ID NO:59, nucleotides 1 to 1302 of SEQ ID NO:59, nucleotides 1 to 1371 of SEQ ID NO:65, and nucleotides 1 to 1302 of SEQ ID NO:65; (ii) the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 500 of SEQ ID NO:1, nucleotides 1 to 500 of SEQ ID NO:3, nucleotides 1 to 500 of SEQ ID NO:5, nucleotides 1 to 500 of SEQ ID NO:7, nucleotides 1 to 500 of SEQ ID NO:9, nucleotides 1 to 500 of SEQ ID NO:11, nucleotides 1 to 500 of SEQ ID NO:13, nucleotides 1 to 500 of SEQ ID NO:15, nucleotides 1 to 500 of SEQ ID NO:37, nucleotides 1 to 500 of SEQ ID NO:39, nucleotides 1 to 500 of SEQ ID NO:41, nucleotides 1 to 500 of SEQ ID NO:43, nucleotides 1 to 500 of SEQ ID NO:45, nucleotides 1 to 500 of SEQ ID NO:47, nucleotides 1 to 500 of SEQ ID NO:49, nucleotides 1 to 500 of SEQ ID NO:51, nucleotides 1 to 500 of SEQ ID NO:53, nucleotides 1 to 500 of SEQ ID NO:55, nucleotides 1 to 500 of SEQ ID NO:57, nucleotides 1 to 500 of SEQ ID NO:59, nucleotides 1 to 500 of SEQ ID NO:65, nucleotides 1 to 221 of SEQ ID NO:17, nucleotides 1 to 239 of SEQ ID NO:18, nucleotides 1 to 199 of SEQ ID NO:19, nucleotides 1 to 191 of SEQ ID NO:20, nucleotides 1 to 232 of SEQ ID NO:21, nucleotides 1 to 467 of SEQ ID NO:22, nucleotides 1 to 534 of SEQ ID NO:23, nucleotides 1 to 563 of SEQ ID NO:24, nucleotides 1 to 218 of SEQ ID NO:25, nucleotides 1 to 492 of SEQ ID NO:26, nucleotides 1 to 481 of SEQ ID NO:27, nucleotides 1 to 463 of SEQ ID NO:28, nucleotides 1 to 513 of SEQ ID NO:29, nucleotides 1 to 579 of SEQ ID NO:30, nucleotides 1 to 514 of SEQ ID NO:31, nucleotides 1 to 477 of SEQ ID NO:32, nucleotides 1 to 500 of SEQ ID NO:33, nucleotides 1 to 470 of SEQ ID NO:34, nucleotides 1 to 491 of SEQ ID NO:35, nucleotides 1 to 221 of SEQ ID NO:36, nucleotides 1 to 519 of SEQ ID NO:61, nucleotides 1 to 497 of SEQ ID NO:62, nucleotides 1 to 498 of SEQ ID NO:63, nucleotides 1 to 525 of SEQ ID NO:64, and nucleotides 1 to 951 of SEQ ID NO:67; and (iii) the complementary strand of the nucleotides selected from the group consisting of: nucleotides 1 to 200 of SEQ ID NO:1, nucleotides 1 to 200 of SEQ ID NO:3, nucleotides 1 to 200 of SEQ ID NO:5, nucleotides 1 to 200 of SEQ ID NO:7, nucleotides 1 to 200 of SEQ ID NO:9, nucleotides 1 to 200 of SEQ ID NO:11, nucleotides 1 to 200 of SEQ ID NO:13, nucleotides 1 to 200 of SEQ ID NO:15, nucleotides 1 to 200 of SEQ ID NO:37, nucleotides 1 to 200 of SEQ ID NO:39, nucleotides 1 to 200 of SEQ ID NO:41, nucleotides 1 to 200 of SEQ ID NO:43, nucleotides 1 to 200 of SEQ ID NO:45, nucleotides 1 to 200 of SEQ ID NO:47, nucleotides 1 to 200 of SEQ ID NO:49, nucleotides 1 to 200 of SEQ ID NO:51, nucleotides 1 to 200 of SEQ ID NO:53, nucleotides 1 to 200 of SEQ ID NO:55, nucleotides 1 to 200 of SEQ ID NO:57, nucleotides 1 to 200 of SEQ ID NO:59, nucleotides 1 to 200 of SEQ ID NO:65, nucleotides 1 to 200 of SEQ ID NO:22, nucleotides 1 to 200 of SEQ ID NO:23, nucleotides 1 to 200 of SEQ ID NO:24, nucleotides 1 to 200 of SEQ ID NO:26, nucleotides 1 to 200 of SEQ ID NO:27, nucleotides 1 to 200 of SEQ ID NO:28, nucleotides 1 to 200 of SEQ ID NO:29, nucleotides 1 to 200 of SEQ ID NO:30, nucleotides 1 to 200 of SEQ ID NO:31, nucleotides 1 to 200 of SEQ ID NO:32, nucleotides 1 to 200 of SEQ ID NO:33, nucleotides 1 to 200 of SEQ ID NO:34, nucleotides 1 to 200 of SEQ ID NO:35, nucleotides 1 to 200 of SEQ ID NO:61, nucleotides 1 to 200 of SEQ ID NO:62, nucleotides 1 to 200 of SEQ ID NO:63, nucleotides 1 to 200 of SEQ ID NO:64, and nucleotides 1 to 200 of SEQ ID NO:67. As will be understood, details and particulars concerning hybridization of the nucleotide sequences will be the same or analogous to the hybridization aspects discussed in the section entitled “Polypeptides Having Cellobiohydrolase I Activity” herein. The present invention also relates to nucleic acid constructs comprising a nucleotide sequence of the present invention operably linked to one or more control sequences that direct the expression of the coding sequence in a suitable host cell under conditions compatible with the control sequences. A nucleotide sequence encoding a polypeptide of the present invention may be manipulated in a variety of ways to provide for expression of the polypeptide. Manipulation of the nucleotide sequence prior to its insertion into a vector may be desirable or necessary depending on the expression vector. The techniques for modifying nucleotide sequences utilizing recombinant DNA methods are well known in the art. The control sequence may be an appropriate promoter sequence, a nucleotide sequence which is recognized by a host cell for expression of the nucleotide sequence. The promoter sequence contains transcriptional control sequences, which mediate the expression of the polypeptide. The promoter may be any nucleotide sequence which shows transcriptional activity in the host cell of choice including mutant, truncated, and hybrid promoters, and may be obtained from genes encoding extracellular or intracellular polypeptides either homologous or heterologous to the host cell. Examples of suitable promoters for directing the transcription of the nucleic acid constructs of the present invention, especially in a bacterial host cell, are the promoters obtained from the Examples of suitable promoters for directing the transcription of the nucleic acid constructs of the present invention in a filamentous fungal host cell are promoters obtained from the genes for In a yeast host, useful promoters are obtained from the genes for The control sequence may also be a suitable transcription terminator sequence, a sequence recognized by a host cell to terminate transcription. The terminator sequence is operably linked to the 3′ terminus of the nucleotide sequence encoding the polypeptide. Any terminator which is functional in the host cell of choice may be used in the present invention. Preferred terminators for filamentous fungal host cells are obtained from the genes for Preferred terminators for yeast host cells are obtained from the genes for The control sequence may also be a suitable leader sequence, a nontranslated region of an mRNA which is important for translation by the host cell. The leader sequence is operably linked to the 5′ terminus of the nucleotide sequence encoding the polypeptide. Any leader sequence that is functional in the host cell of choice may be used in the present invention. Preferred leaders for filamentous fungal host cells are obtained from the genes for Suitable leaders for yeast host cells are obtained from the genes for The control sequence may also be a polyadenylation sequence, a sequence operably linked to the 3′ terminus of the nucleotide sequence and which, when transcribed, is recognized by the host cell as a signal to add polyadenosine residues to transcribed mRNA. Any polyadenylation sequence which is functional in the host cell of choice may be used in the present invention. Preferred polyadenylation sequences for filamentous fungal host cells are obtained from the genes for Useful polyadenylation sequences for yeast host cells are described by Guo and Sherman, 1995, The control sequence may also be a signal peptide coding region that codes for an amino acid sequence linked to the amino terminus of a polypeptide and directs the encoded polypeptide into the cell's secretory pathway. The 5′ end of the coding sequence of the nucleotide sequence may inherently contain a signal peptide coding region naturally linked in translation reading frame with the segment of the coding region which encodes the secreted polypeptide. Alternatively, the 5′ end of the coding sequence may contain a signal peptide coding region which is foreign to the coding sequence. The foreign signal peptide coding region may be required where the coding sequence does not naturally contain a signal peptide coding region. Alternatively, the foreign signal peptide coding region may simply replace the natural signal peptide coding region in order to enhance secretion of the polypeptide. However, any signal peptide coding region which directs the expressed polypeptide into the secretory pathway of a host cell of choice may be used in the present invention. Effective signal peptide coding regions for bacterial host cells are the signal peptide coding regions obtained from the genes for Effective signal peptide coding regions for filamentous fungal host cells are the signal peptide coding regions obtained from the genes for Useful signal peptides for yeast host cells are obtained from the genes for The control sequence may also be a propeptide coding region that codes for an amino acid sequence positioned at the amino terminus of a polypeptide. The resultant polypeptide is known as a proenzyme or propolypeptide (or a zymogen in some cases). A propolypeptide is generally inactive and can be converted to a mature active polypeptide by catalytic or autocatalytic cleavage of the propeptide from the propolypeptide. The propeptide coding region may be obtained from the genes for Where both signal peptide and propeptide regions are present at the amino terminus of a polypeptide, the propeptide region is positioned next to the amino terminus of a polypeptide and the signal peptide region is positioned next to the amino terminus of the propeptide region. It may also be desirable to add regulatory sequences which allow the regulation of the expression of the polypeptide relative to the growth of the host cell. Examples of regulatory systems are those which cause the expression of the gene to be turned on or off in response to a chemical or physical stimulus, including the presence of a regulatory compound. Regulatory systems in prokaryotic systems include the lac, tac, and trp operator systems. In yeast, the ADH2 system or GAL1 system may be used. In filamentous fungi, the TAKA alpha-amylase promoter, The present invention also relates to recombinant expression vectors comprising the nucleic acid construct of the invention. The various nucleotide and control sequences described above may be joined together to produce a recombinant expression vector which may include one or more convenient restriction sites to allow for insertion or substitution of the nucleotide sequence encoding the polypeptide at such sites. Alternatively, the nucleotide sequence of the present invention may be expressed by inserting the nucleotide sequence or a nucleic acid construct comprising the sequence into an appropriate vector for expression. In creating the expression vector, the coding sequence is located in the vector so that the coding sequence is operably linked with the appropriate control sequences for expression. The recombinant expression vector may be any vector (e.g., a plasmid or virus) which can be conveniently subjected to recombinant DNA procedures and can bring about the expression of the nucleotide sequence. The choice of the vector will typically depend on the compatibility of the vector with the host cell into which the vector is to be introduced. The vectors may be linear or closed circular plasmids. The vector may be an autonomously replicating vector, i.e., a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g., a plasmid, an extrachromosomal element, a minichromosome, or an artificial chromosome. The vector may contain any means for assuring self-replication. Alternatively, the vector may be one which, when introduced into the host cell, is integrated into the genome and replicated together with the chromosome(s) into which it has been integrated. Furthermore, a single vector or plasmid or two or more vectors or plasmids which together contain the total DNA to be introduced into the genome of the host cell, or a transposon may be used. The vectors of the present invention preferably contain one or more selectable markers which permit easy selection of transformed cells. A selectable marker is a gene the product of which provides for biocide or viral resistance, resistance to heavy metals, prototrophy to auxotrophs, and the like. Examples of bacterial selectable markers are the dal genes from Preferred for use in an The vectors of the present invention preferably contain an element(s) that permits stable integration of the vector into the host cell's genome or autonomous replication of the vector in the cell independent of the genome. For integration into the host cell genome, the vector may rely on the nucleotide sequence encoding the polypeptide or any other element of the vector for stable integration of the vector into the genome by homologous or nonhomologous recombination. Alternatively, the vector may contain additional nucleotide sequences for directing integration by homologous recombination into the genome of the host cell. The additional nucleotide sequences enable the vector to be integrated into the host cell genome at a precise location(s) in the chromosome(s). To increase the likelihood of integration at a precise location, the integrational elements should preferably contain a sufficient number of nucleotides, such as 100 to 1,500 base pairs, preferably 400 to 1,500 base pairs, and most preferably 800 to 1,500 base pairs, which are highly homologous with the corresponding target sequence to enhance the probability of homologous recombination. The integrational elements may be any sequence that is homologous with the target sequence in the genome of the host cell. Furthermore, the integrational elements may be non-encoding or encoding nucleotide sequences. On the other hand, the vector may be integrated into the genome of the host cell by non-homologous recombination. For autonomous replication, the vector may further comprise an origin of replication enabling the vector to replicate autonomously in the host cell in question. Examples of bacterial origins of replication are the origins of replication of plasmids pBR322, pUC19, pACYC177, and pACYC184 permitting replication in More than one copy of a nucleotide sequence of the present invention may be inserted into the host cell to increase production of the gene product. An increase in the copy number of the nucleotide sequence can be obtained by integrating at least one additional copy of the sequence into the host cell genome or by including an amplifiable selectable marker gene with the nucleotide sequence where cells containing amplified copies of the selectable marker gene, and thereby additional copies of the nucleotide sequence, can be selected for by cultivating the cells in the presence of the appropriate selectable agent. The procedures used to ligate the elements described above to construct the recombinant expression vectors of the present invention are well known to one skilled in the art (see, e.g., Sambrook et al., 1989, supra). The present invention also relates to recombinant a host cell comprising the nucleic acid construct of the invention, which are advantageously used in the recombinant production of the polypeptides. A vector comprising a nucleotide sequence of the present invention is introduced into a host cell so that the vector is maintained as a chromosomal integrant or as a self-replicating extra-chromosomal vector as described earlier. The host cell may be a unicellular microorganism, e.g., a prokaryote, or a non-unicellular microorganism, e.g., a eukaryote. Useful unicellular cells are bacterial cells such as gram positive bacteria including, but not limited to, a The introduction of a vector into a bacterial host cell may, for instance, be effected by protoplast transformation (see, e.g., Chang and Cohen, 1979, The host cell may be a eukaryote, such as a mammalian, insect, plant, or fungal cell. In a preferred embodiment, the host cell is a fungal cell. “Fungi” as used herein includes the phyla Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota (as defined by Hawksworth et al., In a more preferred embodiment, the fungal host cell is a yeast cell. “Yeast” as used herein includes ascosporogenous yeast (Endomycetales), basidiosporogenous yeast, and yeast belonging to the Fungi Imperfecti (Blastomycetes). Since the classification of yeast may change in the future, for the purposes of this invention, yeast shall be defined as described in In an even more preferred embodiment, the yeast host cell is a In a most preferred embodiment, the yeast host cell is a In another more preferred embodiment, the fungal host cell is a filamentous fungal cell. “Filamentous fungi” include all filamentous forms of the subdivision Eumycota and Oomycota (as defined by Hawksworth et al., 1995, supra). The filamentous fungi are characterized by a mycelial wall composed of chitin, cellulose, glucan, chitosan, mannan, and other complex polysaccharides. Vegetative growth is by hyphal elongation and carbon catabolism is obligately aerobic. In contrast, vegetative growth by yeasts such as In an even more preferred embodiment, the filamentous fungal host cell is a cell of a species of, but not limited to, In a most preferred embodiment, the filamentous fungal host cell is an Fungal cells may be transformed by a process involving protoplast formation, transformation of the protoplasts, and regeneration of the cell wall in a manner known per se. Suitable procedures for transformation of The present invention also relates to methods for producing a polypeptide of the present invention comprising (a) cultivating a strain, which in its wild-type form is capable of producing the polypeptide; and (b) recovering the polypeptide. Preferably, the strain is selected from the group consisting of The present invention also relates to methods for producing a polypeptide of the present invention comprising (a) cultivating a host cell under conditions conducive for production of the polypeptide; and (b) recovering the polypeptide. The present invention also relates to methods for in-situ production of a polypeptide of the present invention comprising (a) cultivating a host cell under conditions conducive for production of the polypeptide; and (b) contacting the polypeptide with a desired substrate, such as a cellulosic substrate, without prior recovery of the polypeptide. The term “in-situ production” is intended to mean that the polypeptide is produced directly in the locus in which it is intended to be used, such as in a fermentation process for production of ethanol. In the production methods of the present invention, the cells are cultivated in a nutrient medium suitable for production of the polypeptide using methods known in the art. For example, the cell may be cultivated by shake flask cultivation, small-scale or large-scale fermentation (including continuous, batch, fed-batch, or solid state fermentations) in laboratory or industrial fermentors performed in a suitable medium and under conditions allowing the polypeptide to be expressed and/or isolated. The cultivation takes place in a suitable nutrient medium comprising carbon and nitrogen sources and inorganic salts, using procedures known in the art. Suitable media are available from commercial suppliers or may be prepared according to published compositions (e.g., in catalogues of the American Type Culture Collection). If the polypeptide is secreted into the nutrient medium, the polypeptide can be recovered directly from the medium. If the polypeptide is not secreted, it can be recovered from cell lysates. The polypeptides may be detected using methods known in the art that are specific for the polypeptides. These detection methods may include use of specific antibodies, formation of an enzyme product, or disappearance of an enzyme substrate. For example, an enzyme assay may be used to determine the activity of the polypeptide as described herein. The resulting polypeptide may be recovered by methods known in the art. For example, the polypeptide may be recovered from the nutrient medium by conventional procedures including, but not limited to, centrifugation, filtration, extraction, spray-drying, evaporation, or precipitation. The polypeptides of the present invention may be purified by a variety of procedures known in the art including, but not limited to, chromatography (e.g., ion exchange, affinity, hydrophobic, chromatofocusing, and size exclusion), electrophoretic procedures (e.g., preparative isoelectric focusing), differential solubility (e.g., ammonium sulfate precipitation), SDS-PAGE, or extraction (see, e.g., The present invention also relates to a transgenic plant, plant part, or plant cell which has been transformed with a nucleotide sequence encoding a polypeptide having cellobiohydrolase I activity of the present invention so as to express and produce the polypeptide in recoverable quantities. The polypeptide may be recovered from the plant or plant part. Alternatively, the plant or plant part containing the recombinant polypeptide may be used as such for improving the quality of a food or feed, e.g., improving nutritional value, palatability, and rheological properties, or to destroy an antinutritive factor. The transgenic plant can be dicotyledonous (a dicot) or monocotyledonous (a monocot). Examples of monocot plants are grasses, such as meadow grass (blue grass, Examples of dicot plants are tobacco, lupins, potato, sugar beet, legumes, such as pea, bean and soybean, and cruciferous plants (family Brassicaceae), such as cauliflower, rape, canola, and the closely related model organism Examples of plant parts are stem, callus, leaves, root, fruits, seeds, and tubers. Also specific plant tissues, such as chloroplast, apoplast, mitochondria, vacuole, peroxisomes, and cytoplasm are considered to be a plant part. Furthermore, any plant cell, whatever the tissue origin, is considered to be a plant part. Also included within the scope of the present invention are the progeny (clonal or seed) of such plants, plant parts and plant cells. The transgenic plant or plant cell expressing a polypeptide of the present invention may be constructed in accordance with methods known in the art. Briefly, the plant or plant cell is constructed by incorporating one or more expression constructs encoding a polypeptide of the present invention into the plant host genome and propagating the resulting modified plant or plant cell into a transgenic plant or plant cell. Conveniently, the expression construct is a nucleic acid construct which comprises a nucleotide sequence encoding a polypeptide of the present invention operably linked with appropriate regulatory sequences required for expression of the nucleotide sequence in the plant or plant part of choice. Furthermore, the expression construct may comprise a selectable marker useful for identifying host cells into which the expression construct has been integrated and DNA sequences necessary for introduction of the construct into the plant in question (the latter depends on the DNA introduction method to be used). The choice of regulatory sequences, such as promoter and terminator sequences and optionally signal or transit sequences, is determined, for example, on the basis of when, where, and how the polypeptide is desired to be expressed. For instance, the expression of the gene encoding a polypeptide of the present invention may be constitutive or inducible, or may be developmental, stage or tissue specific, and the gene product may be targeted to a specific tissue or plant part such as seeds or leaves. Regulatory sequences are, for example, described by Tague et al., 1988, For constitutive expression, the 35S-CaMV promoter may be used (Franck et al., 1980, A promoter enhancer element may also be used to achieve higher expression of the enzyme in the plant. For instance, the promoter enhancer element may be an intron which is placed between the promoter and the nucleotide sequence encoding a polypeptide of the present invention. For instance, Xu et al., 1993, supra disclose the use of the first intron of the rice actin 1 gene to enhance expression. The selectable marker gene and any other parts of the expression construct may be chosen from those available in the art. The nucleic acid construct is incorporated into the plant genome according to conventional techniques known in the art, including Presently, Following transformation, the transformants having incorporated therein the expression construct are selected and regenerated into whole plants according to methods well-known in the art. The present invention also relates to methods for producing a polypeptide of the present invention comprising (a) cultivating a transgenic plant or a plant cell comprising a nucleotide sequence encoding a polypeptide having cellobiohydrolase I activity of the present invention under conditions conducive for production of the polypeptide; and (b) recovering the polypeptide. The present invention also relates to methods for in-situ production of a polypeptide of the present invention comprising (a) cultivating a transgenic plant or a plant cell comprising a nucleotide sequence encoding a polypeptide having cellobiohydrolase I activity of the present invention under conditions conducive for production of the polypeptide; and (b) contacting the polypeptide with a desired substrate, such as a cellulosic substrate, without prior recovery of the polypeptide. In a still further aspect, the present invention relates to compositions comprising a polypeptide of the present invention. The composition may comprise a polypeptide of the invention as the major enzymatic component, e.g., a mono-component composition. Alternatively, the composition may comprise multiple enzymatic activities, such as an aminopeptidase, amylase, carbohydrase, carboxypeptidase, catalase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, esterase, alpha-galactosidase, beta-galactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, haloperoxidase, invertase, laccase, lipase, mannosidase, oxidase, pectinolytic enzyme, peptidoglutaminase, peroxidase, phytase, polyphenoloxidase, proteolytic enzyme, ribonuclease, transglutaminase, or xylanase. The compositions may be prepared in accordance with methods known in the art and may be in the form of a liquid or a dry composition. For instance, the polypeptide composition may be in the form of a granulate or a microgranulate. The polypeptide to be included in the composition may be stabilized in accordance with methods known in the art. Examples are given below of preferred uses of the polypeptide compositions of the invention. The dosage of the polypeptide composition of the invention and other conditions under which the composition is used may be determined on the basis of methods known in the art. The polypeptide of the invention may be added to and thus become a component of a detergent composition. The detergent composition of the invention may for example be formulated as a hand or machine laundry detergent composition including a laundry additive composition suitable for pre-treatment of stained fabrics and a rinse added fabric softener composition, or be formulated as a detergent composition for use in general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations. In a specific aspect, the invention provides a detergent additive comprising the polypeptide of the invention. The detergent additive as well as the detergent composition may comprise one or more other enzymes such as a protease, a lipase, a cutinase, an amylase, a carbohydrase, a cellulase, a pectinase, a mannanase, an arabinase, a galactanase, a xylanase, an oxidase, e.g., a laccase, and/or a peroxidase. In general the properties of the chosen enzyme(s) should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts. Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. The protease may be a serine protease or a metallo protease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases are subtilisins, especially those derived from Examples of useful proteases are the variants described in WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially the variants with substitutions in one or more of the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274. Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Other examples are lipase variants such as those described in WO 92/05249, WO 94/01541, EP 407 225, EP 260 105, WO 95/35381, WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202. Suitable amylases (alpha and/or beta) include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Examples of useful amylases are the variants described in WO 94/02597, WO 94/18314, WO 96/23873, and WO 97/43424, especially the variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 181, 188, 190, 197, 202, 208, 209, 243, 264, 304, 305, 391, 408, and 444. Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Especially suitable cellulases are the alkaline or neutral cellulases having colour care benefits. Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940. Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, U.S. Pat. No. 5,457,046, U.S. Pat. No. 5,686,593, U.S. Pat. No. 5,763,254, WO 95/24471, WO 98/12307 and PCT/DK98/00299. Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from The detergent enzyme(s) may be included in a detergent composition by adding separate additives containing one or more enzymes, or by adding a combined additive comprising all of these enzymes. A detergent additive of the invention, i.e., a separate additive or a combined additive, can be formulated e.g., as a granulate, a liquid, a slurry, etc. Preferred detergent additive formulations are granulates, in particular non-dusting granulates, liquids, in particular stabilized liquids, or slurries. Non-dusting granulates may be produced, e.g., as disclosed in U.S. Pat. Nos. 4,106,991 and 4,661,452 and may optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molar weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are given in GB 1483591. Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods. Protected enzymes may be prepared according to the method disclosed in EP 238 216. The detergent composition of the invention may be in any convenient form, e.g., a bar, a tablet, a powder, a granule, a paste or a liquid. A liquid detergent may be aqueous, typically containing up to 70% water and 0-30% organic solvent, or non-aqueous. The detergent composition comprises one or more surfactants, which may be non-ionic including semi-polar and/or anionic and/or cationic and/or zwitterionic. The surfactants are typically present at a level of from 0.1% to 60% by weight. When included therein the detergent will usually contain from about 1% to about 40% of an anionic surfactant such as linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap. When included therein the detergent will usually contain from about 0.2% to about 40% of a non-ionic surfactant such as alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or N-acyl N-alkyl derivatives of glucosamine (“glucamides”). The detergent may contain 0-65% of a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, carbonate, citrate, nitrilotriacetic acid, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g., SKS-6 from Hoechst). The detergent may comprise one or more polymers. Examples are carboxymethylcellulose, poly(vinylpyrrolidone), poly (ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers. The detergent may contain a bleaching system which may comprise a H2O2source such as perborate or percarbonate which may be combined with a peracid-forming bleach activator such as tetraacetylethylenediamine or nonanoyloxybenzenesulfonate. Alternatively, the bleaching system may comprise peroxyacids of e.g., the amide, imide, or sulfone type. The enzyme(s) of the detergent composition of the invention may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g., WO 92/19709 and WO 92/19708. The detergent may also contain other conventional detergent ingredients such as e.g., fabric conditioners including clays, foam boosters, suds suppressors, anti-corrosion agents, soil-suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, hydrotropes, tarnish inhibitors, or perfumes. It is at present contemplated that in the detergent compositions any enzyme, in particular the polypeptide of the invention, may be added in an amount corresponding to 0.01-100 mg of enzyme protein per liter of wash liquor, preferably 0.05-5 mg of enzyme protein per liter of wash liquor, in particular 0.1-1 mg of enzyme protein per liter of wash liquor. The polypeptide of the invention may additionally be incorporated in the detergent formulations disclosed in WO 97/07202 which is hereby incorporated as reference. The nucleotide sequences of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:62, SEQ ID NO:63, SEQ ID NO:64, SEQ ID NO:65, SEQ ID NO:67 may be used in a DNA recombination (or shuffling) process. The new polynucleotide sequences obtained in such a process may encode new polypeptides having cellobiase activity with improved properties, such as improved stability (storage stability, thermostability), improved specific activity, improved pH-optimum, and/or improved tolerance towards specific compounds. Shuffling between two or more homologous input polynucleotides (starting-point polynucleotides) involves fragmenting the polynucleotides and recombining the fragments, to obtain output polynucleotides (i.e., polynucleotides that have been subjected to a shuffling cycle) wherein a number of nucleotide fragments are exchanged in comparison to the input polynucleotides. DNA recombination or shuffling may be a (partially) random process in which a library of chimeric genes is generated from two or more starting genes. A number of known formats can be used to carry out this shuffling or recombination process. The process may involve random fragmentation of parental DNA followed by reassembly by PCR to new full-length genes, e.g., as presented in U.S. Pat. Nos. 5,605,793, 5,811,238, 5,830,721, 6,117,679. In-vitro recombination of genes may be carried out, e.g., as described in U.S. Pat. Nos. 6,159,687, 6,159,688, 5,965,408, 6,153,510, and WO 98/41623. The recombination process may take place in vivo in a living cell, e.g., as described in WO 97/07205 and WO 98/28416. The parental DNA may be fragmented by DNA'se I treatment or by restriction endonuclease digests as described by Kikuchi et al (2000a, Gene 236:159-167). Shuffling of two parents may be done by shuffling single stranded parental DNA of the two parents as described in Kikuchi et al (2000b, A particular method of shuffling is to follow the methods described in Crameri et al, 1998, Production of Ethanol from Biomass The present invention also relates to methods for producing ethanol from biomass, such as cellulosic materials, comprising contacting the biomass with the polypeptides of the invention. Ethanol may subsequently be recovered. The polypeptides of the invention may be produced “in-situ”, i.e., as part of, or directly in an ethanol production process, by cultivating a host cell or a strain, which in its wild-type form is capable of producing the polypeptides, under conditions conducive for production of the polypeptides. Ethanol can be produced by enzymatic degradation of biomass and conversion of the released polysaccharides to ethanol. This kind of ethanol is often referred to as bioethanol or biofuel. It can be used as a fuel additive or extender in blends of from less than 1% and up to 100% (a fuel substitute). In some countries, such as Brazil, ethanol is substituting gasoline to a very large extent. The predominant polysaccharide in the primary cell wall of biomass is cellulose, the second most abundant is hemi-cellulose, and the third is pectin. The secondary cell wall, produced after the cell has stopped growing, also contains polysaccharides and is strengthened through polymeric lignin covalently cross-linked to hemicellulose. Cellulose is a homopolymer of anhydrocellobiose and thus a linear beta-(1-4)-D-glucan, while hemicelluloses include a variety of compounds, such as xylans, xyloglucans, arabinoxylans, and mannans in complex branched structures with a spectrum of substituents. Although generally polymorphous, cellulose is found in plant tissue primarily as an insoluble crystalline matrix of parallel glucan chains. Hemicelluloses usually hydrogen bond to cellulose, as well as to other hemicelluloses, which helps stabilize the cell wall matrix. Three major classes of cellulase enzymes are used to breakdown biomass: The “endo-1,4-beta-glucanases” or 1,4-beta-D-glucan-4-glucanohydrolases (EC 3.2.1.4), which act randomly on soluble and insoluble 1,4-beta-glucan substrates. The “exo-1,4-beta-D-glucanases” including both the 1,4-beta-D-glucan glucohydrolases (EC 3.2.1.74), which liberate D-glucose from 1,4-beta-D-glucans and hydrolyze D-cellobiose slowly, and 1,4-beta-D-glucan cellobiohydrolase (EC 3.2.1.91), also referred to as cellobiohydrolase I, which liberates D-cellobiose from 1,4-beta-glucans. The “beta-D-glucosidases” or beta-D-glucoside glucohydrolases (EC 3.2.1.21), which act to release D-glucose units from cellobiose and soluble cellodextrins, as well as an array of glycosides. These three classes of enzymes work together synergistically in a complex interplay that results in efficient decrystallization and hydrolysis of native cellulose from biomass to yield the reducing sugars which are converted to ethanol by fermentation. The present invention is further described by the following examples which should not be construed as limiting the scope of the invention. Chemicals used as buffers and substrates were commercial products of at least reagent grade. A cDNA library of The full-length CBH1 gene of Several other approaches can be taken: PCR screening of the cDNA library or the cDNAs that were used for the construction of the library, could be performed. To do so, Gene Specific Primers (GSP) and vector/adaptor primers are constructed from the partial cDNA sequence of the CBH1 gene and from vector/adaptor sequence respectively; both sets of primers designed to go outward into the missing 5′ and 3′ regions of the CBH1 cDNA. The longest PCR products obtained using combinations of GSP and vector/adaptor primer represent the full-length 5′ and 3′ end regions of the CBH1 cDNA from Alternatively, the cDNA library could be screened for the full-length cDNA using standard hybridization techniques and the partial cDNA sequence as a probe. The clones giving a positive hybridization signal with the probe are then purified and sequenced to determine the longest cDNA sequence. Homology search and comparison confirms that the full-length cDNA correspond to the partial CBH1 cDNA sequence that was originally used as a probe. The two approaches described above rely on the presence of the full-length CBH1 cDNA in the cDNA library or in the cDNAs used for its construction. Alternatively, the 5′ and 3′ RACE (Rapid Amplification of cDNA Ends) techniques or derived techniques could be used to identify the missing 5′ and 3′ regions. For this purpose, preferably mRNAs from The full-length cDNA of the CBH1 gene from By expression of the full-length gene in a suitable expression host construct the CBH1 enzyme is harvested as an intra cellular or extra cellular enzyme from the culture broth. The methods described above apply to the cloning of cellobiohydrolase I DNA sequences from all organisms and not only A cellobiohydrolase I is characterized by the ability to hydrolyze highly crystalline cellulose very efficiently compared to other cellulases. Cellobiohydrolase I may have a higher catalytic activity using PASO (phosphoric acid swollen cellulose) as substrate than using CMC as substrate. For the purposes of the present invention, any of the following assays can be used to identify a cellobiohydrolase I: Azo-Avicel (Megazyme, Bray Business Park, Bray, Wicklow, Ireland) was used according to the manufacturer's instructions. 50 microliters CBH I solution was mixed with 1 mL substrate solution and incubated 20 minutes at 40° C. The reaction was stopped by addition of 5 mL stop reagent. Absorbance was measured at 404 nm. The substrate is degraded with cellobiohydrolase I (CBH I) to form reducing sugars. A When all components except CBH I are in surplus, the rate of increase in absorbance is proportional to the CBH I activity. The reaction is a one-kinetic-step reaction and may be carried out automatically in a Cobas Fara centrifugal analyzer (Hoffmann La Roche) or another equivalent spectrophotometer which can measure steady state kinetics.
All reagents were added to the buffer in the concentrations indicated above and this reagent solution was mixed thoroughly. 50 microliters cellobiohydrolase I sample (in a suitable dilution) was mixed with 300 μL reagent solution and incubated 20 minutes at 40° C. Purple color formation was detected and measured as absorbance at 550 nm. The AA/TOPS-condensate absorption coefficient is 0.01935 A550/(microM cm). The rate is calculated as micromoles reducing sugar produced per minute from OD550/minute and the absorption coefficient. Acetone and ortho-phosphoric-acid is cooled on ice. Avicel® is moisted with water, and then the 150 mL icecold 85% Ortho-phosphoric-acid is added. The mixture is placed on an icebath with weak stirring for one hour. Add 500 mL ice-cold acetone with stirring, and transfer the mixture to a glass filter funnel and wash with 3×100 mL ice-cold acetone, suck as dry as possible in each wash. Wash with 2×500 mL water (or until there is no odor of acetone), suck as dry as possible in each wash. Re-suspend the solids in water to a total volume of 500 mL, and blend to homogeneity using an Ultra Turrax Homogenizer. Store wet in refrigerator and equilibrate with buffer by centrifugation and re-suspension before use. Bacterial cellulose microfibrils in an impure form were obtained from the Japanese foodstuff “nata de coco” (Fujico Company, Japan). The cellulose in 350 g of this product was purified by suspension of the product in about 4 L of tap water. This water was replaced by fresh water twice a day for 4 days. Then 1% (w/v) NaOH was used instead of water and the product was re-suspended in the alkali solution twice a day for 4 days. Neutralisation was done by rinsing the purified cellulose with distilled water until the pH at the surface of the product was neutral (pH 7). The cellulose was microfibrillated and a suspension of individual bacterial cellulose microfibrils was obtained by homogenisation of the purified cellulose microfibrils in a Waring blender for 30 min. The cellulose microfibrils were further purified by dialysing this suspension through a pore membrane against distilled water and the isolated and purified cellulose microfibrils were stored in a water suspension at 4° C. The following biological material has been deposited under the terms of the Budapest Treaty with the China General Microbiological Culture Collection Center (CGMCC), Institute of Microbiology, Chinese Academy of Sciences, Haidian, Beijing 100080, China:
The following biological material has been deposited under the terms of the Budapest Treaty with the Centraalbureau Voor Schimmelcultures (CBS), Uppsalalaan 8, 3584 CT Utrecht, The Netherlands (alternatively P.O. Box 85167, 3508 AD Utrecht, The Netherlands):
The following biological material has been deposited under the terms of the Budapest Treaty with the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (DSMZ), Mascheroder Weg 1b, 38124 Braunschweig, Germany:
The following biological material has been deposited under the terms of the Budapest Treaty with the Institute for Fermentation, Osaka (IFO), 17-85, Juso-honmachi 2-chome, Yodogawa-ku, Osaka 532-8686, Japan:
The deposit of CBS 427.97, CBS 247.96, CBS 521.95, CBS 284.96, CBS 274.96 were made by Novo Nordisk A/S and were later assigned to Novozymes A/S. The present invention relates to polypeptides having cellobiohydrolase I activity and polynucleotides having a nucleotide sequence which encodes for the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid constructs as well as methods for producing and using the polypeptides. 1-29. (canceled) 30. An isolated polypeptide having cellobiohydrolase I activity, which has at least 80% identity with the sequence of amino acids 1 to 452 of SEQ ID NO:16. 31. The polypeptide of 32. The polypeptide of 33. The polypeptide of 34. The polypeptide of 35. The polypeptide of 36. The polypeptide of 37. The polypeptide of 38. The polypeptide of 39. A detergent composition comprising a surfactant and the polypeptide of 40. A method for producing ethanol from biomass, comprising
(a) contacting the biomass with the polypeptide of (b) fermenting the sugar to produce ethanol.CROSS-REFERENCE TO RELATED APPLICATIONS
FIELD OF THE INVENTION
BACKGROUND OF THE INVENTION
SUMMARY OF THE INVENTION
DEFINITIONS
DETAILED DESCRIPTION OF THE INVENTION
Polypeptides Having Cellobiohydrolase I Activity
Sources for Polypeptides Having Cellobiohydrolase I Activity
Polynucleotides and Nucleotide Sequences
Nucleic Acid Constructs
Expression Vectors
Host Cells
Methods of Production
Plants
Compositions
Detergent Compositions
Proteases:
Lipases:
Amylases:
Cellulases:
Peroxidases/Oxidases:
DNA Recombination (Shuffling)
EXAMPLES
Example 1
Cloning of a Partial and a Full-Length Cellobiohydrolase I (CBH1) DNA Sequence
Example 2
Cellobiohydrolase I (CBH I) Activity
Activity on Azo-Avicel
Activity on PNP-Beta-Cellobiose
Activity on PASO and CMC
PASC:
Materials: 5 g Avicel® (Art. 2331 Merck);
CMC:
Deposit of Biological Material
China General Microbiological Culture Collection Center (CGMCC)
Centraalbureau Voor Schimmelcultures (CBS)
Deutsche Sammlunq von Mikroorganismen und Zellkulturen GmbH (DSMZ)
Institute for Fermentation, Osaka (IFO)