Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Cloning and Characterization of a ${\beta}$-Glucosidase from Marine Microbial Metagenome with Excellent Glucose Tolerance

  • Fang, Zemin (School of Life Sciences and Biotechnology Center, Anhui University) ;
  • Fang, Wei (School of Life Sciences and Biotechnology Center, Anhui University) ;
  • Liu, Juanjuan (School of Life Sciences and Biotechnology Center, Anhui University) ;
  • Hong, Yuzhi (School of Life Sciences and Biotechnology Center, Anhui University) ;
  • Peng, Hui (School of Life Sciences and Biotechnology Center, Anhui University) ;
  • Zhang, Xuecheng (School of Life Sciences and Biotechnology Center, Anhui University) ;
  • Sun, Baolin (School of Life Sciences, University of Science and Technology of China) ;
  • Xiao, Yazhong (School of Life Sciences and Biotechnology Center, Anhui University)
  • Received : 2010.03.04
  • Accepted : 2010.06.07
  • Published : 2010.09.28
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Abstract

The demand for ${\beta}$-glucosidases insensitive to product inhibition is increasing in modern biotechnology, for these enzymes would improve the process of saccharification of lignocellulosic materials. In this study, a ${\beta}$-glucosidase gene that encodes a 442-amino-acid protein was isolated from a marine microbial metagenomic library by functional screening and named as bgl1A. The protein was identified to be a member of the glycoside hydrolases 1 family, and was recombinantly expressed, purified, and biochemically characterized. The recombinant ${\beta}$-glucosidase, Bgl1A, exhibited a high level of stability in the presence of various cations and high concentrations of NaCl. Interestingly, it was activated by glucose at concentrations lower than 400 mM. With glucose further increasing, the enzyme activity of Bgl1A was gradually inhibited, but remained 50% of the original value in even as high as 1,000 mM glucose. These findings indicate that Bgl1A might be a potent candidate for industrial applications.

Keywords

References

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