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Cloning, Expression, and Characterization of ${eta}$-glucosidase from Exiguobacterium sp. DAU5 and Transglycosylation Activity
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  • Cloning, Expression, and Characterization of ${eta}$-glucosidase from Exiguobacterium sp. DAU5 and Transglycosylation Activity
  • Cloning, Expression, and Characterization of ${eta}$-glucosidase from Exiguobacterium sp. DAU5 and Transglycosylation Activity
저자명
Chang. Jie,Park. In-Hye,Lee. Yong-Seok,Ahn. Soon-Cheol,Zhou. Yi,Choi. Yong-Lark
간행물명
Biotechnology and bioprocess engineering
권/호정보
2011년|16권 1호|pp.97-106 (10 pages)
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한국생물공학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

A gram-negative bacterium, designated strain DAU5, was isolated from shrimp shell samples because it demonstrated high ${eta}$-glucosidase activity. Through 16S rDNA gene sequence analysis the strain was identified as belonging to the genus Exiguobacterium. The ${eta}$-glucosidase gene of Exiguobacterium sp. DAU5 was successfully cloned by the shotgun method. Nucleotide sequence determination by sodium dodecyl sulfate-ployacrylamide gel electrophoresis indicated that the gene for the enzyme contained 1,350 bp, was coded by 450 amino acids, and was 52 kDa. The polypeptide exhibits significant homology with other bacterial ${eta}$-glucosidases and belongs to the Glycoside Hydrolase Family 1. The ${eta}$-glucosidase was purified by a His-fusion purification system. The optimal pH and temperature of the enzyme were 7.0 and $45^{circ}C$, respectively. The enzyme activity was strongly inhibited by $Ca^{2+}$, and $Li^+$, $K^+$, $Zn^{2+}$, $Mg^{2+}$, $Na^{2+}$, $Ni^{2+}$, and EDTA partially inhibited the enzyme activity. The BglA showed the highest activity with p-NPG and MUG. However, strain DAU5 ${eta}$-glucosidase, which is for degradation of oligosaccharides, is expected to be useful for the fermentation of cellulose degradation and the transglycosylation of saccharides.