TECHNOLOGY FOCUS - BIOLOGY - Preferred Components: The biomass is corn stover, bagasses, sorghum, giant reed, elephant grass, miscanthus, Japanese cedar, wheat straw, switchgrass, hardwood pulp, softwood pulp, crushed sugar cane, energy cane, or Napier grass. The recombinant cell is a eukaryotic cell, filamentous fungal cell; or yeast cell. The filamentous fungal cell is of the genus Aspergillus, Penicillium, Rhizopus, Chrysosporium, Myceliophthora, Trichoderma, Humicola, Acremonium or Fusarium (preferably selected from species Aspergillus niger, Aspergillus oryzae, Trichoderma reesei, Penicillium chrysogenum, Myceliophthora thermophila, or Rhizopus oryzae. The yeast cell is of the genus Saccharomyces, Kluyveromyces, Candida, Pichia, Schizosaccharomyces, Hansenula, Klockera, Schwanniomyces or Yarrowia (preferably selected from species Saccharomyces cerevisiae, Saccharomyces bulderi, Saccharomyces barnetti, Saccharomyces exiguus, Saccharomyces uvarum, Saccharomyces diastaticus, Kluyveromyces lactis, Kluyveromyces marxianus or Kluyveromyces fragilis, especially Saccharomyces cerevisiae cell). The fermenting microorganism is a bacterium or a yeast. The bacterium is selected from Zymomonas mobilis, Escherichia coli and Klebsiella oxytoca. The yeast is selected from Saccharomyces cerevisiae, Saccharomyces uvarum, Kluyveromyces fragilis, Kluyveromyces lactis, Candida pseudotropicalis, and Pachysolen tannophilus. The vector further comprises an origin of replication; a promoter sequence operably linked to the nucleotide sequence. The promoter sequence is operable in yeast; is operable in filamentous fungi. The host cell is a prokaryotic cell; bacterial cell; or eukaryotic cell.    TECHNOLOGY FOCUS - BIOTECHNOLOGY - Recombinant Methods (Claimed): Producing (M3) the polypeptide involving: culturing a recombinant cell engineered to express the polypeptide under conditions in which the polypeptide is expressed. In the method (M3), when the polypeptide comprises a signal sequence, then the recombinant cell is cultured under conditions in which the polypeptide is secreted from the recombinant cell. The method (M3) further involves: recovering the polypeptide from the cell culture. The recovering the polypeptide involves: centrifuging away cells and/or cellular debris; filtering away cells and/or cellular debris. The variant CBH II polypeptide having increased specific activity as compared to a reference CBH II polypeptide is prepared by: either modifying the nucleotide sequence of a CBH II-encoding nucleic acid so that the nucleic acid encodes a variant CBH II polypeptide, where the variant CBH II polypeptide comprises at least one amino acid substitution selected from: Ile235Val substitution; Pro64Trp substitution; Pro64Glu substitution; Leu21Arg substitution; Ser104Val substitution; Gly37Ser substitution; Gly65Leu substitution; Lys309His substitution; Glu66Arg substitution; Ser115Ala substitution; Gly67Lys substitution; Glu23Lys substitution; Ser115Met substitution; Ala33Lys substitution; or Glu23Asn substitution; and expressing the variant CBH II polypeptide, thus generating a variant CBH II polypeptide having increased specific activity as compared to a reference CBH II polypeptide; or modifying the nucleotide sequence of a CBH II-encoding nucleic acid so that the nucleic acid encodes a variant CBH II polypeptide, where the variant CBH II polypeptide comprises: Asp194Asn substitution; Ala200Leu substitution; Ser421Cys substitution; Asp426Asn substitution; Ala429Ser substitution; Thr430Pro substitution; Tyr434Ala substitution; Ala438Leu substitution; Ser439Pro substitution; Ala440Asp substitution; Leu442Thr substitution; Gln443Pro substitution; and Pro444Asn substitution; and expressing the variant CBH II polypeptide, thus generating a variant CBH II polypeptide having increased specific activity as compared to a reference CBH II polypeptide. The modification is by site directed mutagenesis. Preferred Components: The polypeptide further comprises a variant CBH II cellulose binding domain, where the cellulose binding domain has at least one amino acid substitutions selected from Gly37Ser substitution; and Ala33Lys substitution; variant CBH II SS linker sequence, where the SS linker sequence has at least one amino acid substitutions selected from Leu21Arg substitution; Glu23Lys substitution; and Glu23Asn substitution; a variant CBH II CBD-CD linker sequence, where the CBD-CD linker sequence has at least one amino acid substitutions selected from: Pro64Trp substitution; Pro64Glu substitution; Gly65Leu substitution; Glu66Arg substitution; and Gly67Lys substitution. The catalytic domain has a Asp194Asn substitution, Ala200Leu substitution, Ser421Cys substitution, Asp426Asn substitution, Ala429Ser substitution, Thr430Pro substitution, Tyr434Ala substitution, Ala438Leu substitution, Ser439Pro substitution, Ala440Asp substitution, Leu442Thr substitution, Gln443Pro substitution, and Pro444Asn substitution. The polypeptide has a CBH II specific activity that is at least 2%, at least 3%, at least 4%, at least 5%, at least 10%, at least 15%, at least 20%, at least 25% or at least 30% greater than the specific activity of a reference CBH II which does not have the same substitution(s). The polypeptide comprises a catalytic domain and a cellulose binding domain. The catalytic domain is operably linked to the cellulose binding domain via a CBD-CD linker. In the polypeptide, the cellulose binding domain is C-terminal to the catalytic domain; SS-linker N-terminal to the catalytic domain; the cellulose binding domain is N-terminal to the catalytic domain. The SS-linker is N-terminal to the cellulose binding domain. The polypeptide comprises an amino acid sequence having at least 60% sequence, preferably at least 70%, more preferably at least 80%, especially at least 90%, or particularly at least 95% sequence identity to defined amino acid sequence having 468 amino acids (SEQ ID NO: 2) as given in the specification. The other than the substitution comprises sequence of (SEQ ID NO: 2). The polypeptide which is a mature polypeptide. The mature polypeptide comprises an amino acid sequence having at least 90%, at least 95% or at least 97% sequence identity of the mature portion of a polypeptide according to any one of 132 sequences given in the specification (SEQ ID NO: 2) to (SEQ ID NO: 133) e.g. defined amino acid sequence having 447 amino acids (SEQ ID NO: 37) as given in the specification, defined amino acid sequence having 348 amino acids (SEQ ID NO: 122) as given in the specification as, defined amino acid sequence having 423 amino acids (SEQ ID NO: 123) as given in the specification, defined amino acid sequence having 443 amino acids (SEQ ID NO: 124) as given in the specification or defined amino acid sequence having 390 amino acids (SEQ ID NO: 125) as given in the specification. The polypeptide further comprises a signal sequence. The polypeptide which upon expression produces a mature polypeptide comprising an amino acid sequence having at least 90%, at least 95% or at least 97% sequence identity of the mature portion of a polypeptide according to any one of the (SEQ ID NO: 2) to (SEQ ID NO: 133). The fermentation broth is a filamentous fungal fermentation broth; or cell-free fermentation broth. Preferred Composition: The composition comprises at least 1%, preferably at least 5%, especially at least 25% of all polypeptides in the composition. The composition is a whole cellulase; is produced by a host cell that recombinantly expresses the polypeptide; is filamentous fungal whole cellulase. Preferred Method: The method (M1) further involves: recovering fermentable sugars. The method (M2) further involves: prior to first step, pretreating the biomass.    TECHNOLOGY FOCUS - ORGANIC CHEMISTRY - Preferred Components: The fermentable sugars comprise disaccharides, monosaccharides. The monosaccharides are produced by a beta -glucosidase in the composition or the fermentation broth. The fermentation product is ethanol. EXAMPLE - No suitable example given.