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Heterologous expression and characterization of a novel halotolerant, thermostable, and alkali-stable GH6 endoglucanase from Thermobifida halotolerans
- Yin, Yi-Rui, Zhang, Feng, Hu, Qing-Wen, Xian, Wen-Dong, Hozzein, Wael N., Zhou, En-Min, Ming, Hong, Nie, Guo-Xing, Li, Wen-Jun
- Biotechnology letters 2015 v.37 no.4 pp. 857-862
- Thermobifida, endo-1,4-beta-glucanase, genes, glycosides, industrial applications, molecular weight, pH, salt tolerance, sodium chloride, thermal stability
- A novel endoglucanase gene was cloned from Thermobifida halotolerans YIM 90462ᵀ, 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.