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KMID : 1094720070120030265
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Biotechnology and Bioprocess Engineering
2007 Volume.12 No. 3 p.265 ~ p.270
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Purification and characterization of thermostable β-1,3-1,4 glucanase from Bacillus sp. A8-8
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Jung Youn-Ju
Yoo Ju-Soon
Lee Yong-Seok
Park In-Hye
Kim Sun-Hee
Lee Sang-Cheol
Yasuda Masaaki
Chung Soo-Yeol
Choi Yong-Lark
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Abstract
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In this study, the extracellular enzyme activity ofBacillus sp. A8-8 was detected on LB agar plates containing 0.5% of the following substrates: carboxymethylcellulose (CMC), xylan, cellulose, and casein, respectively. The β-1,3-1,4 glucanase produced fromBacillus sp. A8-8 was purified by ammonium sulfate and hydrophobic chromatography. The molecular size of the protein was estimated by SDS-PAGE as approximately 33 kDa. The optimum pH and temperature for the enzyme activity were 6.0 and 60°C, respectiveley. However, enzyme activity was shown over a broad range of pH values and temperatures. The purified β-1,3-1,4 glucanase retained over 70% of its original activity after incubation at 80°C for 2 h, and showed over 40% of its original activity within the pH range of 9 to 12. This suggests that β-1,3-1,4 glucanase fromBacillus sp. A8-8 is thermostable and alkalistable. In addition, β-1,3-1,4 glucanase had higher substrate specificity to lichenan than to CMC. Finally the activity of the endoglucanase was inhibited by Fe3+, Mg2+, and Mn2+ ions. However Co2+ and Ca2+ ions were increased its activity.
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KEYWORD
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Bacillus subtilis, β-1, 3-1, 4 glucanase, CMC-SDS-PAGE, agar-diffusion test
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