Abstract
A heat-stable enzyme was isolated from the cellulase complex of a thermophilic strain of the micromyceteThielavia terrestris. The purified enzyme exhibited both endoglucanase and xylanase activities and had a mol mass of 69,000 Daltons and an isoelectric point of 6.4. When the cells were grown at 48°C, the initial activity of the purified enzyme using carboxymethylcellulose as a substrate was 150 nkat/mg and the Michaelis constant was 6.6 g/L. The heat stability of the enzyme was high, losing only 20% of the initial activity after a 6-h incubation at 65 °C. When cultures were grown on microcrystalline cellulose and xylose was added after 48 h of growth, endoglucanase and xylanase activities were more than doubled. Similar increases in these activities were observed by growing the cultures on straw.
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Abbreviations
- CMC:
-
carboxymethyl cellulose
- MCC:
-
microcrystalline cellulose
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Kvesitadze, E.G., Lomitashvili, T.B., Khutsishvili, M.P. et al. Isolation and properties of a thermostable endoglucanase from a thermophilic mutant strain ofTielavia terrestris . Appl Biochem Biotechnol 50, 137–143 (1995). https://doi.org/10.1007/BF02783450
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DOI: https://doi.org/10.1007/BF02783450