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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제26권 제11호
- 발행연도
- 2016.1
- 수록면
- 1,933 - 1,942 (10page)
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초록· 키워드
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A novel α-glucoside hydrolase (named PspAG97A) from glycoside hydrolase family 97 (GH97) was cloned from the deep-sea bacterium Pseudoalteromonas sp. K8, which was screened from the sediment of Kongsfjorden. Sequence analysis showed that PspAG97A belonged to GH97, and shared 41% sequence identity with the characterized α-glucosidase BtGH97a. PspAG97A possessed three key catalytically related glutamate residues. Mutation of the glutamate residues indicated that PspAG97A belonged to the inverting subfamily of GH97. PspAG97A showed significant reversibility against changes in salt concentration. It exhibited halophilic ability and improved thermostability in NaCl solution, with maximal activity at 1.0 M NaCl/KCl, and retained more than 80% activity at NaCl concentrations ranging from 0.8 to 2.0 M for over 50 h. Furthermore, PspAG97A hydrolyzed not only α-1,4-glucosidic linkage, but also α-1,6- and α-1,2-glucosidic linkages. Interestingly, PspAG97A possessed high catalytic efficiency for long-chain substrates with α-1,6-linkage. These characteristics are clearly different from other known α-glucoside hydrolases in GH97, implying that PspAG97A is a unique α-glucoside hydrolase of GH97.
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참고문헌 (21)
참고문헌 신청
Arnosti C. / 2011 / Microbial extracellular enzymes and the marine carbon cycle / Annu. Rev. Mar. Sci 3:401~425
Boutaiba S / 2006 / Preliminary characterisation of a lipolytic activity from an extremely halophilic archaeon, Natronococcus sp / J. Mol. Catal. B Enzym 41:21~26
Henrissat B / 1997 / Structural and sequence-based classification of glycoside hydrolases / Curr. Opin. Struct. Biol 7:637~644
Hough DW / 1999 / Extremozymes / Curr. Opin. Chem. Biol 3:39~46
Hughes C / 2003 / Cloning and expression of α-D-glucosidase and Nacetyl-β-glucosaminidase from the periodontal pathogen, Tannerella forsythensis (Bacteroides forsythus) / Oral Microbiol. Immunol 18:309~312
Boutaiba S / 2006 / Preliminary characterisation of a lipolytic activity from an extremely halophilic archaeon, Natronococcus sp / J. Mol. Catal. B Enzym 41:21~26
Henrissat B / 1997 / Structural and sequence-based classification of glycoside hydrolases / Curr. Opin. Struct. Biol 7:637~644
Hough DW / 1999 / Extremozymes / Curr. Opin. Chem. Biol 3:39~46
Hughes C / 2003 / Cloning and expression of α-D-glucosidase and Nacetyl-β-glucosaminidase from the periodontal pathogen, Tannerella forsythensis (Bacteroides forsythus) / Oral Microbiol. Immunol 18:309~312
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