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Title 

Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil

 

신규 저온활성 에스터레이스

Authors 

Kyong Cheol KoSoon Ok RimYunjon HanB S ShinG J KimJong Hyun ChoiJae Jun Song

Publisher 

Springer

Issue Date 

2012

Citation 

Journal of Industrial Microbiology (& Biotechnology), vol. 39, no. 5, pp. 681-689

Keywords 

CloningCold-adapted esteraseExpressionMetagenomic libraryScreening

Abstract 

A novel lipolytic enzyme was isolated from a metagenomic library after demonstration of lipolytic activity on an LB agar plate containing 1% (w/v) tributyrin. A novel esterase gene (estIM1), encoding a lipolytic enzyme (EstIM1), was cloned using a shotgun method from a pFos- EstIM1 clone of the metagenomic library, and the enzyme was characterized. The estIM1 gene had an open reading frame (ORF) of 936 base pairs and encoded a protein of 311 amino acids with a molecular mass 34 kDa and a pI value of 4.32. The deduced amino acid sequence was 62% identical to that of an esterase from an uncultured bacterium (ABQ11271). The amino acid sequence indicated that EstIM1 was a member of the family IV of lipolytic enzymes, all of which contain a GDSAG motif shared with similar enzymes of lactic acid microorganisms. EstIM1 was active over atemperature range of 1-50C°, at alkaline pH. The activation energy for hydrolysis of p-nitrophenyl propionate was 1.04 kcal/mol, within a temperature range of 1-40C°. The activity of EstIM1 was about 60% of maximal even at 1C°, suggesting that EstIM1 is eYciently coldadapted. Further characterization of this cold-adapted enzyme indicated that the esterase may be very valuable in industrial applications.

ISSN 

0169-4146

Link 

http://dx.doi.org/10.1007/s10295-011-1080-y

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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