Purification and characterization of thermostable β-1,3-1,4 glucanase from<Emphasis Type="Italic">Bacillus</Emphasis> sp. A8-8 |
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Authors: | Youn-Ju Jung Ju-Soon Yoo Yong-Seok Lee In-Hye Park Sun-Hee Kim Sang-Cheol Lee Masaaki Yasuda Soo-Yeol Chung Yong-Lark Choi |
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Institution: | (1) Department of Biotechnology, Faculty of Natural Resources and Life Sciences, Dong-A University, 604-614 Busan, Korea;(2) Department of Bioscience and Biotechnology, Faculty of Agriculture, Ryukyus University, 903-0213 Okinawa, Japan;(3) Department of Food Science and Nutrition, Dongju College, 604-715 Busan, Korea |
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Abstract: | 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.
These authors contributed equally to this work. |
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Keywords: | Bacillus subtilis β -1 3-1 4 glucanase CMC-SDS-PAGE agar-diffusion test |
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