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자료유형
학술저널
저자정보
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한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제16권 제1호
발행연도
2006.1
수록면
145 - 148 (4page)

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A new functional lipolytic enzyme (AT4) has recentlybeen found from Agrobacterium tumefaciens C58 Cereonusing a genome-wide approach. The enzyme has some sequencesimilarity to E. coli acetyl hydrolase, Emericella nidulanslipase, Moraxella sp. lipase, Acinetobacter lwoffi esterase,and Streptomyces hygroscopicus acetyl hydrolase. However,the sequence similarities are very low (less than 25%),suggesting that it is a new lipase/esterase enzyme. In the presentstudy, intact cell of the A. tumefaciens strain was shown towas then expressed at a high level in E. coli BL21 (DE3) cellsand the enzyme was purified simply by Ni-NTA columnchromatography. The purified enzyme showed hydrolyticactivity toward p-nitrophenyl caproate, but not toward oliveoil, suggesting that the AT4 enzyme was a typical esteraserather than lipase. AT4 esterase had a maximum hydrolyticactivity at 45oC and pH 8.0, when p-nitrophenyl caproateoC andat pH 5.0-9.0. Calcium ion and EDTA did not affect theactivity and thermal stability of the enzyme. As for substratespecificity, AT4 enzyme could rapidly hydrolyze acetyl andbutyl groups from p-nitrophenyl esters and 1-naphthyl esters.In adition, it also released acetyl residues from acetylatedglucose and xylose substrates. Therefore, this new esteraseenzyme might be used as a biocatalyst in acetylation and

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