Properties and gene structure of a bifunctional cellulolytic enzyme (CelA) from the extreme thermophile 'Anaerocellum thermophilum' with separate glycosyl hydrolase family 9 and 48 catalytic domains

Article Abstract:

A large cellulolytic enzyme (CelA) which can hydrolyze microcrystalline cellulose was extracted from the extremely thermophilic, cellulolytic bacterium 'Anaerocellum thermophilum.' The enzyme had significant activity towards Avicel and was most active towards soluble substrates. The enzyme was found to be most closely related to CelA of Caldicellulosiruptor saccharolyticus. Because of the substantially improved Avicelase activity of full-length CelA, exoglucanase activity may be attributed to the C-terminal family 48 catalytic domain.

Genetic aspects, Bacteria, Thermophilic, Microbial enzymes, Cellulose, Thermophiles

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Polythionate degradation by tetrathionate hydrolase of Thiobacillus ferrooxidans

Article Abstract:

The hydrolysis of polythionate by cell-free extracts of Thiobacillus ferrooxidans and the purification of tetrathionate hydrolase were presented. Tetrathionate hydrolase is the enzyme responsible for hydrolysis which was purified to homogeneity using the spectrophotometric assay. Thiosulfate, sulfur and sulfate were the end products of polythionate degradation. The enzyme activity was measured during the purification procedure which is based on the increase of absorbance in the UV region.

Enzymes, Bacillus (Bacteria), Bacillus

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