TECHNOLOGY FOCUS - BIOTECHNOLOGY - Isolation (Claimed): The enzyme is isolated from Deinococcus or its related bacterium. Preferred Enzyme: The enzyme is active at temperature of 30 degrees C or more, preferably 40 degrees C or more. The enzyme catalyzes biomass modification and is chosen from amylase, glucosidase, cellulase, xylanase, pectinase, esterase, acetyl xylan esterase or glucuronidase and comprises all or an active portion, such as mature form without signal peptide, of an amino acid sequence of SEQ ID NOs: 1-12, 58, 60, 64, 66, 68, 70 and 72. The enzyme preferably acetaldehyde dehydrogenase, alcohol dehydrogenase or pyruvate dehydrogenase is involved in biofuel production and comprises all or an active portion of an amino acid sequence of SEQ ID NOs: 27-41. Preferred Cell: The recombinant cell is Deinococcus or its related bacterium. Sequences not defined here may be found at ftp://ftp.wipo.int/pub/published_pct_sequences/publication. EXAMPLE - Bacteria i.e. Deinococcus were inoculated on minimal culture medium. The growth of the bacteria was monitored. The cell-free culture supernatants were tested either for their ability to release reducing sugar monomer (glucose) from starch. The Deinococcus strain M23r-2A was found to grow rapidly in the presence of starch as sole carbon source. The alpha -amylase enzyme was identified in the above-mentioned strain. Nucleic acid encoding alpha -amylase was derived from Deinococcus strain M23r-2A comprising sequence of SEQ ID NO: 3 and cloned into pETDEST42 vector using standard recombinant methodology. The nucleic acid was cloned in frame with 6(His) tag to facilitate purification of recombinant protein. The recombinant nucleic acid was transformed into Escherichia coli and cultured in Luria Bertani medium (4 l). The production of the alpha -amylase protein was induced overnight at 30 degrees C in presence of 1 mM isopropyl beta -D-thiogalactopyranoside (IPTG). The cultured medium was subjected to centrifugation, collected cells were resuspended in solution comprising tris(hydroxymethyl)aminomethane hydrochloride (Tris-HCl) buffer (50 mM) of pH 8, sodium chloride (300 mM), imidazole (5 mM), glycerine (5%), phenylmethanesulfonylfluoride (PMSF) (0.5 mM), and lysozyme (l mg/ml). The cells were disrupted by sonication. The cell debris were removed by centrifugation and supernatant was collected and subjected to HisTrap (RTM: High performance column) affinity chromatography column. Fractions containing recombinant alpha -amylase were eluted with buffer containing imidazole (300 mM), sodium chloride (300 mM), Tris-HCl (50 mM, pH 8) and dialyzed against Tris-HCl (50 mM, pH 8), sodium chloride (50 mM), and glycerine (5%). The alpha -amylase having molecular weight of 49 kDa derived from M23r-2A was purified to 90% homogeneity with yield of 4 mg/l of culture.