TECHNOLOGY FOCUS - BIOTECHNOLOGY - Preparation (Disclosed): The recombinant Bg11 variant is prepared by standard recombinant methods. Preferred Amino acid: The recombination Bg11 variant comprises amino acid substitutions Q291, D369 and E402, preferably Q291W, D369R and E402N. The recombinant Bg11 variant further comprises amino acid substitutions chosen from Q258N/II, Q313M, S434, A475, K495, G628, Q258, Q313, S434, A475, K495, and G628. The amino acid substitutions are Q258N/11, Q313M, S434P, A475L, K495N, and G628W. The recombinant variant comprises amino acid substitutions A689 or Y715, A689I or Y715P, A689I or Y715P, A475L, or D47, A343 or T687. The recombinant Bg11 variant comprises at least one amino acid substitution D47, A343C or T687W/K/C, D47I, A343C and T687K, or I106, V260, F314 or A732. The recombinant variant comprises amino acid substitutions I106V, V260G, F314L/V or A732G/M/V, F314V/L or A732G, A79, Q85, A109 or A343, or D47I, A79E, A79F/G/M, Q85N or A109T/S. The recombinant Bg11 variant further comprises amino acid substitutions A79E, Q85N, A109S, and A79M. The recombinant Bg11 variant has (a) increased thermo stability after incubation at pH 5 at 65 degrees c for six months relative to wild-type Bg11 comprising amino acid residues at position 20-870 of SEQ ID NO: 2, (b) increased thermo activity for the above condition for 21 hours and (c) both (a) and (b). Preferred Composition: The enzyme composition further comprises recombinant endoglucanase (EG) polypeptide, recombinant cellobiohydrolase polypeptide (CBH) or recombinant EG polypeptide and recombinant CBH polypeptide, at least one polypeptide selected from hemicellulase, pectinase, lignin peroxidase, manganese peroxidase, laccase, and cellobiose dehydrogenase. The enzyme composition further comprises host cell expressing recombinant Bg11 variant. EXAMPLE - Wild-type C1 beta -glucosidase 1 (C1 Bgl1) cDNA was synthesized and the DNA sequence was verified. The gene was cloned into a Saccharomyces cerevisiae C1 shuttle vector pYTDX20 using Pml1 cloning sites. The signal peptide and gene were under the control of a chitinase promoter (Pchi). The vector contained the REP2, rep1 and protein D (partial) origin of replication for S.cerevisiae and a URA3 resistance marker. The resulting plasmid (pYTDX20-C1 bgl1) was transformed into S.cerevisiae strain INVSC1, and the transformed host cells were grown in helical tubular photo bioreactor (HTP) for C1 Bgl1 protein production. The C1 bgl1 sequence from the transformants was verified. Single colony of S.cerevisiae containing a plasmid with the C1 bgl1 cDNA gene was inoculated into 1 ml synthetic defined-uracil (SD-ura) broth (synthetic prop-out minus uracil w/o yeast nitrogen base (in g/l) (2), ammonium sulfate (5), calcium chloride (0.1), inositol (2 mg/l), magnesium sulfate (0.5), potassium phosphate monobasic (1) and sodium chloride (0.1)) containing 6% glucose. Cells were grown for 24 hours in an incubator at 30 degrees C with shaking at 250 revolutions per minute (rpm). Overnight culture (500 mu l) was then diluted into SD-ura media (50 ml) containing 2% glucose in a 250 ml baffled sterile shake flask and incubated at 37 degrees C for 48 hours. Cells were pelleted by centrifugation (4000 rpm, 15 minutes, 4 degrees C). The clear media supernatant containing the secreted C1 Bgl1 enzyme was collected and stored at ?20 degrees C for further use.