Journal of Microbiology and Biotechnology

  • 제18권9호
  • /
  • Pages.1544-1549
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  • 2008
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지

Bifunctional Recombinant Fusion Enzyme Between Maltooligosyltrehalose Synthase and Maltooligosyltrehalose Trehalohydrolase of Thermophilic Microorganism Metallosphaera hakonensis

  • Seo, Ju-Seok (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University) ;
  • An, Ju-Hee (Department of Food and Nutrition, Seowon University) ;
  • Cheong, Jong-Joo (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University) ;
  • Choi, Yang-Do (Department of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University) ;
  • Kim, Chung-Ho (Department of Food and Nutrition, Seowon University)
  • 발행 : 2008.09.30
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초록

MhMTS and MhMTH are trehalose ($\alpha$-D-glucopyranosyl-[1,1]-$\alpha$-D-glucopyranose) biosynthesis genes of the thermophilic microorganism Metallosphaera hakonensis, and encode a maltooligosyltrehalose synthase (MhMTS) and a maltooligosyltrehalose trehalohydrolase (MhMTH), respectively. In this study, the two genes were fused in-frame in a recombinant DNA, and expressed in Escherichia coli to produce a bifunctional fusion enzyme, MhMTSH. Similar to the two-step reactions with MhMTS and MhMTH, the fusion enzyme catalyzed the sequential reactions on maltopentaose, maltotriosyltrehalose formation, and following hydrolysis, producing trehalose and maltotriose. Optimum conditions for the fusion enzyme-catalyzed trehalose synthesis were around $70^{\circ}C$ and pH 5.0-6.0. The MhMTSH fusion enzyme exhibited a high degree of thermostability, retaining 80% of the activity when pre-incubated at $70^{\circ}C$ for 48 h. The stability was gradually abolished by incubating the fusion enzyme at above $80^{\circ}C$. The MhMTSH fusion enzyme was active on various sizes of maltooligosaccharides, extending its substrate specificity to soluble starch, the most abundant natural source of trehalose production.

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참고문헌

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