Novel metagenome-derived, cold-adapted alkaline phospholipase with superior lipase activity as an intermediate between phospholipase and lipase

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dc.contributor.authorMi Hwa Lee-
dc.contributor.authorK H Oh-
dc.contributor.authorChul Hyung Kang-
dc.contributor.authorJ H Kim-
dc.contributor.authorTae Kwang Oh-
dc.contributor.authorChoong-Min Ryu-
dc.contributor.authorJ H Yoon-
dc.date.accessioned2017-04-19T09:32:10Z-
dc.date.available2017-04-19T09:32:10Z-
dc.date.issued2012-
dc.identifier.issn0099-2240-
dc.identifier.uri10.1128/AEM.00260-12ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10807-
dc.description.abstractA novel lipolytic enzyme was isolated from a metagenomic library obtained from tidal flat sediments on the Korean west coast. Its putative functional domain, designated MPlaG, showed the highest similarity to phospholipase A from Grimontia hollisae CIP 101886, though it was screened from an emulsified tricaprylin plate. Phylogenetic analysis showed that MPlaG is far from family I.6 lipases, including Staphylococcus hyicus lipase, a unique lipase which can hydrolyze phospholipids, and is more evolutionarily related to the bacterial phospholipase A 1 family. The specific activitiesof MPlaG against olive oil and phosphatidylcholine were determined to be 2,957 ± 144 and 1,735 ± 147Umg -1, respectively, which means that MPlaG is a lipid-preferred phospholipase. Among different synthetic esters, triglycerides, and phosphatidylcholine, purified MPlaG exhibited the highest activity toward p-nitrophenyl palmitate (C 16), tributyrin (C 4), and 1,2-dihexanoyl-phosphatidylcholine (C 8). Finally, MPlaG was identified as a phospholipase A 1 with lipase activity by cleavage of the sn-1 position of OPPC, interfacial activity, and triolein hydrolysis. These findings suggest that MPlaG is the first experimentally characterized phospholipase A 1 with lipase activity obtained from a metagenomic library. Our study provides an opportunity to improve our insight into the evolution of lipases and phospholipases.-
dc.publisherAmer Soc Microb-
dc.titleNovel metagenome-derived, cold-adapted alkaline phospholipase with superior lipase activity as an intermediate between phospholipase and lipase-
dc.title.alternativeNovel metagenome-derived, cold-adapted alkaline phospholipase with superior lipase activity as an intermediate between phospholipase and lipase-
dc.typeArticle-
dc.citation.titleApplied and Environmental Microbiology-
dc.citation.number14-
dc.citation.endPage4966-
dc.citation.startPage4959-
dc.citation.volume78-
dc.contributor.affiliatedAuthorMi Hwa Lee-
dc.contributor.affiliatedAuthorChul Hyung Kang-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.affiliatedAuthorChoong-Min Ryu-
dc.contributor.alternativeName이미화-
dc.contributor.alternativeName오기훈-
dc.contributor.alternativeName강철형-
dc.contributor.alternativeName김지훈-
dc.contributor.alternativeName오태광-
dc.contributor.alternativeName류충민-
dc.contributor.alternativeName윤정훈-
dc.identifier.bibliographicCitationApplied and Environmental Microbiology, vol. 78, no. 14, pp. 4959-4966-
dc.identifier.doi10.1128/AEM.00260-12-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Research on National Challenges > Infectious Disease Research Center > 1. Journal Articles
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