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KMID : 0364820100460010068
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Korean Journal of Microbiology
2010 Volume.46 No. 1 p.68 ~ p.72
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Characterization of Bacillus licheniformis B1 β-1,4-Glucanase Overproduced in Escherichia coli
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Song Hye-Jung
Hwang Jae-Sung
Kim Han-Bok
Kim Hwang-Yeon
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Abstract
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The β-1,4-glucanase gene of Bacillus licheniformis B1 was expressed in Esherichia coli BL21, and a protein with a mass of 50 kDa that was soluble was overproduced. A protein with a mass of 37 kDa was secreted from B. licheniformis. It seems that the β-1,4-glucanase produced in E. coli contained the leader peptide and unprocessed carboxy-terminal region, but its processing occurred in the carboxyterminal in Bacillus. The optimal temperature of β-1,4-glucanase was 40°C. The enzyme still had 76% maximal activity at 60°C. The optimal pH of the enzyme was 7. The enzyme retained considerable activities over the weak-acidic, neutral, and weak-basic pH range. Acidic fungal cellulases are used in
food, detergent, pulp, paper, textile industries. However, studies about neutral and alkaline cellulase are not enough. The cellulase developed in this study may be useful for industrial applications in the fields of biofuel development.
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KEYWORD
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B. licheniformis, β-1, 4-glucanase, cellulase, E. coli
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