NOVELTY - A family 5 glycoside hydrolase variant having a mutated version of a wild-type parental polypeptide with at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 91%, 98% or greater than or equal to 99%, or complete sequence identity to specified amino acid sequence and comprising specific amino acid residue changes, is new.    USE - For hydrolyzing cellulose (claimed), and producing fuel (including ethanol, methanol, propanol and/or butanol).    ADVANTAGE - The present cellulase variants show improved performance, in particular with respect to increased catalytic activity and/or altered thermostability. Particularly the present family 5 glycoside hydrolase variant having endoglucanase activity, also achieves improved properties, such as improved hydrolysis rates, better thermal stability, reduced adsorption to lignin, and the ability to hydrolyze non-cellulosic components of biomass, such as hemicellulose, in addition to hydrolyzing cellulose. These endoglucanases with a broad range of side activities on hemicellulose are beneficial for improving the overall hydrolysis yield of complex, hemicellulose-rich biomass substrates.    DETAILED DESCRIPTION - A mature family 5 glycoside hydrolase variant (v1) having a mutated version of a wild-type parental polypeptide with at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or greater than or equal to 99%, or complete sequence identity to an amino acid sequence of (SEQ ID NO: 2) as available on WIPO website and comprising at least one of the following amino acid residue changes: proline is substituted with serine at position 53; proline is substituted with histidine at position 59; proline is substituted with lysine at position 59; threonine is substituted with proline at position 61; lysine is substituted with asparagine at position 64; glycine is substituted with methionine at position 70; threonine is substituted with histidine at position 87; threonine is substituted with methionine at position 87; glycine is substituted with alanine at position 92; serine is substituted with leucine at position 183; threonine is substituted with glutamic acid at position 184; lysine is substituted with asparagine at position 192; glutamine is substituted with alanine at position 197; lysine is substituted with methionine at position 199; serine is substituted with valine at position 200; and lysine is substituted with alanine at position 300, where the variant has at least one of the following activities: endoglucanase activity, a beta-mannanase activity, an exo-1,3-glucanase activity, an endo-1,6-glucanase activity, a xylanase activity and an endoglycoceramidase activity, and the activity of the variant is greater than the wild-type parental polypeptide having an amino acid sequence of (SEQ ID NO: 2). Sequences not defined here may be found at ftp://ftp.wipo.net/pub/published pct sequences/publication. INDEPENDENT CLAIMS are included for the following:    (1) mutated version of a wild-type parental polynucleotide encoding family 5 glycoside hydrolase variant, having at least 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 91%, 98% or greater than or equal to 99%, or complete sequence identity to a (cDNA) nucleotide sequence of (SEQ ID NO: 1) as available on WIPO website and comprising at least one of following nucleotide residue changes: the nucleotides at positions 157 to 159 are tct; the nucleotides at positions 175 to 177 are aag; the nucleotides at positions 175 to 177 are cat; the nucleotides at positions 181 to 183 are cct; the nucleotides at positions 190 to 192 are aat; the nucleotides at positions 208 to 210 are atg; the nucleotides at positions 259 to 261 are cat; the nucleotides at positions 259 to 261 are atg; the nucleotides at positions 274 to 276 are gct; the nucleotides at positions 547 to 549 are ttg; the nucleotides at positions 550 to 552 are gag; the nucleotides at positions 574 to 576 are aat; the nucleotides at positions 589 to 591 are gct; the nucleotides at positions 595 to 597 are atg; the nucleotides at positions 598 to 600 are gtt; and the nucleotides at positions 898 to 900 are gcg, is new. The variant has at least one of the following activities: endoglucanase activity, a beta-mannanase activity, an exo-1,3-glucanase activity, an endo-1,6-glucanase activity, a xylanase activity, and an endoglycoceramidase activity. The activity of the variant is greater than a polypeptide encoded by the wild-type parental polynucleotide having a nucleotide sequence of (SEQ ID NO: 1);    (2) an expression cassette, a vector or a cloning vehicle comprising the mutated version of a wild-type parental polynucleotide sequence (SEQ ID NO: 1), where optionally the cloning vehicle comprises a viral vector, a plasmid, a phage, a phagemid, a cosmid, a fosmid, a bacteriophage or an artificial chromosome, and optionally the viral vector comprises an adenovirus vector, a retroviral vector or an adeno-associated viral vector, and optionally the cloning vehicle comprises a bacterial artificial chromosome (BAC), a plasmid, a bacteriophage PI-derived vector (PAC), a yeast artificial chromosome (YAC), or a mammalian artificial chromosome (MAC);    (3) a transformed cell comprising a nucleic acid comprising the mutated version of a wild-type parental polynucleotide sequence (SEQ ID NO: 1), where optionally the cell is a bacterial cell, a mammalian cell, a fungal cell, a yeast cell, an insect cell or a plant cell;    (4) a transformed cell comprising the expression vector; and    (5) hydrolyzing cellulose comprising contacting biomass with the polypeptide.