Abstract

A novel endoglucanase gene was cloned from Thermobifida halotolerans YIM 90462(T), designated as thcel6A for being a member of glycoside hydrolase family 6. The gene was 1332 bp long and encoded a 443-amino-acid protein with a molecular mass of 45.9 kDa. The purified recombinant endoglucanase had optimal activity at 55 °C and pH 8.5. Thcel6A showed high hydrolytic activities at 25-55 °C and retained 58% of initial activity after incubation at 90 °C for 1 h. It retained more than 80% of activity after incubation for 12 h at pH values from 4 to 12. Thcel6A displayed higher hydrolytic activities in 5-15% NaCl (w/v) than at 0% NaCl. Activity increased 2.5-fold after incubation with 20% (w/v) NaCl at 37 °C for 10 min. These properties suggest that this novel endoglucanase has potential for specific industrial application.

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