Molecular Cloning, Overexpression, and Enzymatic Characterization of Glycosyl Hydrolase Family 16 β-Agarase from Marine Bacterium Saccharophagus sp. AG21 in Escherichia coli
분야
자연과학 > 생물
저자
( Young Deuk Lee ) , ( Chul Hong Oh ) , ( Mahanama De Zoysa ) , ( Hyo Won Kim ) , ( Wickramaarachchige Don Niroshana Wickramaarachchi ) , ( Ilson Whang ) , ( Do Hyung Kang ) , ( Je Hee Lee )
발행기관
한국미생물생명공학회(구 한국산업미생물학회)
간행물정보
Journal of Microbiology and Biotechnology 2013년, 제23권 제7호, 913~922페이지(총10페이지)
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05212306.pdf [무료 PDF 뷰어 다운로드]
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    영문초록
    An agar-degrading bacterium was isolated from red seaweed (Gelidium amansii) on a natural seawater agar plate, and identified as Saccharophagus sp. AG21. The β-agarase gene from Saccharophagus sp. AG21 (agy1) was screened by long and accurate (LA)-PCR. The predicted sequence has a 1,908 bp open reading frame encoding 636 amino acids (aa), and includes a glycosyl hydrolase family 16 (GH16) β-agarase module and two carbohydrate binding modules of family 6 (CBM6). The deduced aa sequence showed 93.7% and 84.9% similarity to β-agarase of Saccharophagus degradans and Microbulbifer agarilyticus, respectively. The mature agy1 was cloned and overexpressed as a His-tagged recombinant β-agarase (rAgy1) in Escherichia coli, and had a predicted molecular mass of 69 kDa and an isoelectric point of 4.5. rAgy1 showed optimum activity at 55oC and pH 7.6, and had a specific activity of 85 U/mg. The rAgy1 activity was enhanced by FeSO4 (40%), KCl (34%), and NaCl (34%), compared with the control. The newly identified rAgy1 is a β-agarase, which acts to degrade agarose to neoagarotetraose (NA4) and neoagarohexaose (NA6) and may be useful for applications in the cosmetics, food, bioethanol, and reagent industries.
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