Characterization of a novel esterase isolated from intertidal flat metagenome and its tertiary alcohols synthesis

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• 作者：Ki-Hoon Oh^a ; Giang-Son Nguyen^b ; Eun-Young Kim^a ; Robert Kourist^c ; Uwe Bornscheuer^b ; Tae-Kwang Oh^a ; Jung-Hoon Yoon^d ; ^{jhyoon69@skku.edu}
• 关键词：Metagenome ; Esterase ; HSL family ; Tertiary alcohol synthesis
• 刊名：Journal of Molecular Catalysis B ; Enzymatic
• 出版年：2012
• 期刊代码：55_13811177
• 类别：ce
• 出版时间：August, 2012
• 卷：80
• 期：Complete
• 页码：67-73
• 文件大小：769 K

摘要

A gene coding for an esterase (EstEH112) was isolated from metagenome originated from Korean intertidal flat sediment. The putative esterase gene encoded a 340 amino acids protein with characteristic residues of lipolytic enzymes such as a conserved pentapeptide (GXSXG), the typical catalytic S-D-H triad, and a GGG(A)X-motif in the oxyanion hole near the active site similar to the hormone sensitive lipase (HSL) family. p-Nitrophenyl butyrate was the best substrate for the enzyme among the other p-nitrophenyl esters investigated. The apparent optimal temperature and pH for EstEH112 was 35 掳C and at pH 8.0, respectively. EstEH112 efficiently catalyzed the hydrolysis of various large tertiary alcohol esters. These characteristics of EstEH112 make it a potential candidate for application in biocatalysis.