Enzymatic Properties of a Thermostable α-Glucosidase from Acidothermophilic Crenarchaeon Sulfolobus tokodaii Strain 7
분야
자연과학 > 생물
저자
( Jung Eun Park ) , ( So Hae Park ) , ( Jung Yoon Woo ) , ( Hye Sun Hwang ) , ( Jae Ho Cha ) , ( Hee Seob Lee )
발행기관
한국미생물생명공학회(구 한국산업미생물학회)
간행물정보
Journal of Microbiology and Biotechnology 2013년, 제23권 제1호, 56~63페이지(총8페이지)
파일형식
05212125.pdf [무료 PDF 뷰어 다운로드]
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    영문초록
    We have characterized the putative α-glucosidase gene (st2525) selected by total genome analysis from the acidothermophilic crenarchaeon Sulfolobus tokodaii strain 7. The ORF was cloned and expressed as a fusion protein in Escherichia coli, and recombinant ST2525 was purified by Ni-NTA affinity chromatography. Maximum activity was observed at 95oC and pH 4.0, and the enzyme exhibited stability with half-lives of 40.1 min and 7.75 min at extremely high temperatures of 100oC and 105oC, respectively. The enzyme retained at least 85% of its maximal activity in the pH range of 4.0-11.0. ST2525 exclusively hydrolyzed α-1,4-glycosidic linkages of oligosaccharides in an exo-type manner, with highest catalytic efficiency toward maltotriose. The enzyme also displayed transglycosylation activity, converting maltose to isomaltose, panose, maltotriose, isomaltotriose, etc. From these results, ST2525 could be potentially useful for starch hydrolysis as well as novel synthesis of oligosaccharides in industry.
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