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

Ki Hoon Oh; Giang Son Nguyen; Eun Young Kim; Robert Kourist; Uwe Bornscheuer; Tae Kwang Oh; Jung Hoon Yoon

doi:10.1016/j.molcatb.2012.04.015

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

Ki Hoon Oh
, Giang Son Nguyen
, Eun Young Kim
, Robert Kourist
, Uwe Bornscheuer
, Tae Kwang Oh
, Jung Hoon Yoon

Department of Food Science and Biotechnology

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	67-73
Number of pages	7
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	80
DOIs	https://doi.org/10.1016/j.molcatb.2012.04.015
State	Published - Aug 2012

Keywords

Esterase
HSL family
Metagenome
Tertiary alcohol synthesis

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10.1016/j.molcatb.2012.04.015

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title = "Characterization of a novel esterase isolated from intertidal flat metagenome and its tertiary alcohols synthesis",

abstract = "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.",

keywords = "Esterase, HSL family, Metagenome, Tertiary alcohol synthesis",

author = "Oh, \{Ki Hoon\} and Nguyen, \{Giang Son\} and Kim, \{Eun Young\} and Robert Kourist and Uwe Bornscheuer and Oh, \{Tae Kwang\} and Yoon, \{Jung Hoon\}",

year = "2012",

month = aug,

doi = "10.1016/j.molcatb.2012.04.015",

language = "English",

volume = "80",

pages = "67--73",

journal = "Journal of Molecular Catalysis B: Enzymatic",

issn = "1381-1177",

publisher = "Elsevier",

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TY - JOUR

T1 - Characterization of a novel esterase isolated from intertidal flat metagenome and its tertiary alcohols synthesis

AU - Oh, Ki Hoon

AU - Nguyen, Giang Son

AU - Kim, Eun Young

AU - Kourist, Robert

AU - Bornscheuer, Uwe

AU - Oh, Tae Kwang

AU - Yoon, Jung Hoon

PY - 2012/8

Y1 - 2012/8

N2 - 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.

AB - 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.

KW - Esterase

KW - HSL family

KW - Metagenome

KW - Tertiary alcohol synthesis

UR - https://www.scopus.com/pages/publications/84861334373

U2 - 10.1016/j.molcatb.2012.04.015

DO - 10.1016/j.molcatb.2012.04.015

M3 - Article

AN - SCOPUS:84861334373

SN - 1381-1177

VL - 80

SP - 67

EP - 73

JO - Journal of Molecular Catalysis B: Enzymatic

JF - Journal of Molecular Catalysis B: Enzymatic

ER -

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

Abstract

Keywords

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