Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Functional Expression of Amylosucrase, a Glucan-Synthesizing Enzyme, from Arthrobacter chlorophenolicus A6

  • Seo, Dong-Ho (Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University) ;
  • Jung, Jong-Hyun (Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University) ;
  • Choi, Hyun-Chang (Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University) ;
  • Cho, Hyun-Kuk (Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University) ;
  • Kim, Hee-Hang (Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University) ;
  • Ha, Suk-Jin (Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University) ;
  • Yoo, Sang-Ho (Department of Food Science and Technology, and Carbohydrate Bioproduct Research Center, Sejong University) ;
  • Cha, Jaeho (Department of Microbiology, College of Natural Sciences, Pusan National University) ;
  • Park, Cheon-Seok (Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University)
  • Received : 2012.01.31
  • Accepted : 2012.05.01
  • Published : 2012.09.28
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Abstract

A gene (acas) designated as ${\alpha}$-amylase was cloned from Arthrobacter chlorophenolicus A6. The multiple amino acid sequence analysis and functional expression of acas revealed that this gene really encoded an amylosucrase (ASase) instead of ${\alpha}$-amylase. In fact, the recombinant enzyme exhibited typical ASase activity by showing both sucrose hydrolysis and glucosyltransferase activities. The purified enzyme has a molecular mass of 72 kDa and exhibits optimal hydrolysis activity at $45^{\circ}C$ and a pH of 8.0. The analysis of the oligomeric state of ACAS with gel permeation chromatography revealed that the ACAS existed as a monomer.

Keywords

References

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