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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제19권 제3호
- 발행연도
- 2009.1
- 수록면
- 257 - 264 (8page)
이용수
초록· 키워드
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A β-agarase gene, agaB34, was functionally cloned from
the genomic DNA of a marine bacterium, Agarivorans albus
YKW-34. The open reading frame of agaB34 consisted of
1,362 bp encoding 453 amino acids. The deduced amino acid
sequence, consisting of a typical N-terminal signal peptide
followed by a catalytic domain of glycoside hydrolase family
16 (GH-16) and a carbohydrate-binding module (CBM),
showed 37-86% identity to those of agarases belonging to
family GH-16. The recombinant enzyme (rAgaB34) with
a molecular mass of 49 kDa was produced extracellularly
using Escherichia coli DH5α as a host. The purified rAgaB34
was a β-agarase yielding neoagarotetraose (NA4) as the
main product. It acted on neoagarohexaose to produce NA4
and neoagarobiose, but it could not further degrade NA4.
The maximal activity of rAgaB34 was observed at 30oC and
pH 7.0. It was stable over pH 5.0-9.0 and at temperatures
up to 50oC. Its specific activity and kcat/Km value for agarose
were 242 U/mg and 1.7×106/sM, respectively. The activity
of rAgaB34 was not affected by metal ions commonly existing
in seawater. It was resistant to chelating reagents (EDTA,
EGTA), reducing reagents (DTT, β-mercaptoethanol), and
denaturing reagents (SDS and urea). The E. coli cell harboring
the pUC18-derived agarase expression vector was able to
efficiently excrete agarase into the culture medium. Hence,
this expression system might be used to express secretory
proteins.
목차
등록된 정보가 없습니다.
참고문헌 (22)
참고문헌 신청
Aoki, T. / 1990 / Purification and characterization of a novel β-agarase from Vibrio sp. AP-2 / Eur. J. Biochem 187 : 461 ~ 465
Araki, C. H. / 1937 / Acetylation of agar-like substance of Gelidium amansii / J. Chem. Soc. Japan 58 : 1338 ~ 1350
Araki, T. / 1998 / Optimization of parameters for isolation of protoplasts from Gracilaria verrucosa (Rhodophyta) / J. Mar. Biotechnol 6 : 193 ~ 197
Bradford, M. M. / 1976 / A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72
Dong, J. / 2007 / A unique β-agarase, AgaA, from a marine bacterium, Vibrio sp. strain PO-303 / Appl. Microbiol. Biotechnol 74 : 1248 ~ 1255
Araki, C. H. / 1937 / Acetylation of agar-like substance of Gelidium amansii / J. Chem. Soc. Japan 58 : 1338 ~ 1350
Araki, T. / 1998 / Optimization of parameters for isolation of protoplasts from Gracilaria verrucosa (Rhodophyta) / J. Mar. Biotechnol 6 : 193 ~ 197
Bradford, M. M. / 1976 / A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72
Dong, J. / 2007 / A unique β-agarase, AgaA, from a marine bacterium, Vibrio sp. strain PO-303 / Appl. Microbiol. Biotechnol 74 : 1248 ~ 1255
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