4.4 Article

Mechanism of substrate hydrolysis by a thermophilic endoglucanase from Thermotoga maritima

Journal

BIOTECHNOLOGY LETTERS
Volume 22, Issue 9, Pages 735-740

Publisher

SPRINGER
DOI: 10.1023/A:1005656203233

Keywords

cellulase; hyperthermophile; mechanism; synergy

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A cellulase from the thermophile, Thermotoga maritima, hydrolyzed oligosaccharide substrates by an exoglucanase mode of action but acted as an endoglucanase to rapidly reduce the Viscosity of the soluble polysaccharides carboxymethylcellulose and barley beta-glucan. The V-max for hydrolysis of the substrate, p-nitrophenyl beta-D-cellobioside, was 42 mu mol min(-1) (mg protein)(-1), while that for barley beta-glucan was 637. The enzyme had little activity on crystalline cellulose.

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