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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제26권 제6호
- 발행연도
- 2016.1
- 수록면
- 1,087 - 1,097 (11page)
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초록· 키워드
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An intracellular lipase from Anoxybacillus flavithermus HBB 134 was purified to 7.4-fold. The molecular mass of the enzyme was found to be about 64 kDa. The maximum activity of the enzyme was at pH 9.0 and 50oC. The enzyme was stable between pH 6.0 and 11.0 at 25°C, 40°C, and 50°C for 24 h. The Km and Vmax of the enzyme for pNPL substrate were determined as 0.084 mM and 500 U/mg, respectively. Glycerol, sorbitol, and mannitol enhanced the enzyme thermostability. The enzyme was found to be highly stable against acetone, ethyl acetate, and diethyl ether. The presence of PMSF, NBS, DTT and β-mercaptoethanol inhibited the enzyme activity. Hg2+, Fe3+, Pb2+, Al3+, and Zn2+ strongly inhibited the enzyme whereas Li+, Na+, K+, and NH4 + slightly activated it. At least 60% of the enzyme activity and stability were retained against sodium deoxycholate, sodium taurocholate, n-octyl-β-D-glucopyranoside, and CHAPS. The presence of 1% Triton X-100 caused about 34% increase in the enzyme activity. The enzyme is thought to be a true lipase since it has preferred the long-chain triacylglycerols. The lipase of HBB 134 cleaved triolein at the 1- or 3-position.
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참고문헌 (45)
참고문헌 신청
Andualema B / 2012 / Microbial lipases and their industrial applications: review / Biotechnology 11:100~118
Ay F / 2011 / Cloning, purification and characterization of a thermostable carboxylesterase from Anoxybacillus sp. PDF / Protein Expr. Purif 80:74~79
Bakir ZB / 2015 / Screening for industrially important enzymes from thermophilic bacteria; selection of lipaseproducing microorganisms and optimization of culture conditions / Eur. J. Biotechnol. Biosci 3:43~48
Bornscheuer UT / 2002 / Microbial carboxyl esterases:classification, properties and application in biocatalysis / FEMS. Microbiol. Rev 26:73~81
Bradford MM / 1976 / Arapid and s ensitiv e method f or the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72:248~254
Ay F / 2011 / Cloning, purification and characterization of a thermostable carboxylesterase from Anoxybacillus sp. PDF / Protein Expr. Purif 80:74~79
Bakir ZB / 2015 / Screening for industrially important enzymes from thermophilic bacteria; selection of lipaseproducing microorganisms and optimization of culture conditions / Eur. J. Biotechnol. Biosci 3:43~48
Bornscheuer UT / 2002 / Microbial carboxyl esterases:classification, properties and application in biocatalysis / FEMS. Microbiol. Rev 26:73~81
Bradford MM / 1976 / Arapid and s ensitiv e method f or the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72:248~254
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