Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 80, Issue -, Pages 67-73Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2012.04.015
Keywords
Metagenome; Esterase; HSL family; Tertiary alcohol synthesis
Funding
- Ministry of Education, Science and Technology (MEST) of the Republic of Korea [MG05-0401-2-0]
- European Social Funds
- VentureCup M-V [UG09005]
- DAAD [A/07/95194]
- Vietnamese ministry of Education and Training [3413/QDBGDDT-VP]
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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 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. (C) 2012 Elsevier B.V. All rights reserved.
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