A novel family VII esterase with industrial potential from compost metagenomic library

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dc.contributor.authorChul Hyung Kang-
dc.contributor.authorKi Hoon Oh-
dc.contributor.authorMi Hwa Lee-
dc.contributor.authorTae Kwang Oh-
dc.contributor.authorB H Kim-
dc.contributor.authorJung-Hoon Yoon-
dc.date.accessioned2017-04-19T09:25:13Z-
dc.date.available2017-04-19T09:25:13Z-
dc.date.issued2011-
dc.identifier.issn1475-2859-
dc.identifier.uri10.1186/1475-2859-10-41ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10301-
dc.description.abstractBackground: Among the vast microbial genomic resources now available, most microbes are unculturable in the laboratory. A culture-independent metagenomic approach is a novel technique that circumvents this culture limitation. For the screening of novel lipolytic enzymes, a metagenomic library was constructed from compost, and the clone of estCS2 was selected for lipolytic properties on a tributyrin-containing medium.Results: The estCS2 sequence encodes a protein of 570 amino acid residues, with a predicted molecular mass of 63 kDa, and based on amino acid identity it most closely matches (45%) the carboxylesterase from Haliangium ochraceum DSM 14365. EstCS2 belong to family VII, according to the lipolytic enzyme classification proposed by Arpigny and Jaeger, and it retains the catalytic triad Ser245-Glu363-His466that is typical of an α/β hydrolase. The Ser245residue in the catalytic triad of EstCS2 is located in the consensus active site motif GXSXG. The EstCS2 exhibits strong activity toward p-nitrophenyl caproate (C6), and it is stable up to 60°C with an optimal enzymatic activity at 55°C. The maximal activity is observed at pH 9, and it remains active between pH 6-10. EstCS2 shows remarkable stability in up to 50% (v/v) dimethyl sulfoxide (DMSO) or dimethylformamide (DMF). The enzyme has the ability to cleave sterically hindered esters of tertiary alcohol, as well as to degrade polyurethanes, which are widely used in various industries.Conclusions: The high stability of EstCS2 in organic solvents and its activity towards esters of ketoprofen and tertiary alcohols, and in polyurethane suggests that it has potential uses for many applications in biotransformation and bioremediation.-
dc.publisherSpringer-BMC-
dc.titleA novel family VII esterase with industrial potential from compost metagenomic library-
dc.title.alternativeA novel family VII esterase with industrial potential from compost metagenomic library-
dc.typeArticle-
dc.citation.titleMicrobial Cell Factories-
dc.citation.number0-
dc.citation.endPage41-
dc.citation.startPage41-
dc.citation.volume10-
dc.contributor.affiliatedAuthorChul Hyung Kang-
dc.contributor.affiliatedAuthorKi Hoon Oh-
dc.contributor.affiliatedAuthorMi Hwa Lee-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.affiliatedAuthorJung-Hoon Yoon-
dc.contributor.alternativeName강철형-
dc.contributor.alternativeName오기훈-
dc.contributor.alternativeName이미화-
dc.contributor.alternativeName오태광-
dc.contributor.alternativeName김봉희-
dc.contributor.alternativeName윤정훈-
dc.identifier.bibliographicCitationMicrobial Cell Factories, vol. 10, pp. 41-41-
dc.identifier.doi10.1186/1475-2859-10-41-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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