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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제30권 제11호
- 발행연도
- 2020.1
- 수록면
- 1,659 - 1,669 (11page)
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이 논문의 연구 히스토리 (2)
2020
해양미생물 Gayadomonas joobiniege G7이 생산하는 1,3-α-3,6-anhydro-L-galactosidase 효소의 분자생물학적 연구
서주원
생명과학정보학과
2020.01
학위논문
Molecular Characterization of a Novel 1,3-α-3,6-Anhydro-L-Galactosidase, Ahg943, with Cold- and High-Salt-Tolerance from Gayadomonas joobiniege G7
서주원
,
Tsevelkho
,
loo Ma
외 6명
Journal of Microbiology and Biotechnology
2020.01
학술저널
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초록· 키워드
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1,3-α-3,6-anhydro-L-galactosidase (α-neoagarooligosaccharide hydrolase) catalyzes the last step of agar degradation by hydrolyzing neoagarobiose into monomers, D-galactose, and 3,6-anhydro-Lgalactose, which is important for the bioindustrial application of algal biomass. Ahg943, from the agarolytic marine bacterium Gayadomonas joobiniege G7, is composed of 423 amino acids (47.96 kDa), including a 22-amino acid signal peptide. It was found to have 67% identity with the α-neoagarooligosaccharide hydrolase ZgAhgA, from Zobellia galactanivorans, but low identity (< 40%) with the other α-neoagarooligosaccharide hydrolases reported. The recombinant Ahg943 (rAhg943, 47.89 kDa), purified from Escherichia coli, was estimated to be a monomer upon gel filtration chromatography, making it quite distinct from other α-neoagarooligosaccharide hydrolases. The rAhg943 hydrolyzed neoagarobiose, neoagarotetraose, and neoagarohexaose into D-galactose, neoagarotriose, and neoagaropentaose, respectively, with a common product, 3,6- anhydro-L-galactose, indicating that it is an exo-acting α-neoagarooligosaccharide hydrolase that releases 3,6-anhydro-L-galactose by hydrolyzing α-1,3 glycosidic bonds from the nonreducing ends of neoagarooligosaccharides. The optimum pH and temperature of Ahg943 activity were 6.0 and 20°C, respectively. In particular, rAhg943 could maintain enzyme activity at 10°C (71% of the maximum). Complete inhibition of rAhg943 activity by 0.5 mM EDTA was restored and even, remarkably, enhanced by Ca2+ ions. rAhg943 activity was at maximum at 0.5 M NaCl and maintained above 73% of the maximum at 3M NaCl. Km and Vmax of rAhg943 toward neoagarobiose were 9.7 mg/ml and 250 μM/min (3 U/mg), respectively. Therefore, Ahg943 is a unique α-neoagarooligosaccharide hydrolase that has cold- and high-salt-adapted features, and possibly exists as a monomer.
목차
등록된 정보가 없습니다.
참고문헌 (40)
참고문헌 신청
Altschul SF / 1997 / Gapped BLAST and PSI-BLAST : a new generation of protein database search programs / Nucleic Acids Res 25:3389~3402
Araki C / 1959 / Carbohydrate chemistry of substances of biological interests / Pergamon Press :15~30
Asghar S / 2019 / Molecular cloning and characterization of a novel cold-adapted alkaline 1, 3-α-3, 6-anhydro-l-galactosidase, Ahg558, from Gayadomonas joobiniege G7 / Appl. Biochem. Biotechnol 188:1077~1095
Asghar S / 2018 / Identification and biochemical characterization of a novel coldadapted 1, 3-a-3, 6-anhydro-L-galactosidase, Ahg786, from Gayadomonas joobiniege G7 / Appl. Microbiol. Biotechnol 102:8855~8866
Bradford MM / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72:248~254
Araki C / 1959 / Carbohydrate chemistry of substances of biological interests / Pergamon Press :15~30
Asghar S / 2019 / Molecular cloning and characterization of a novel cold-adapted alkaline 1, 3-α-3, 6-anhydro-l-galactosidase, Ahg558, from Gayadomonas joobiniege G7 / Appl. Biochem. Biotechnol 188:1077~1095
Asghar S / 2018 / Identification and biochemical characterization of a novel coldadapted 1, 3-a-3, 6-anhydro-L-galactosidase, Ahg786, from Gayadomonas joobiniege G7 / Appl. Microbiol. Biotechnol 102:8855~8866
Bradford MM / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72:248~254
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