Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1

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dc.contributor.authorHyung Kwoun Kim-
dc.contributor.authorSun Yang Park-
dc.contributor.authorJung Kee Lee-
dc.contributor.authorTae Kwang Oh-
dc.date.accessioned2017-04-19T08:55:20Z-
dc.date.available2017-04-19T08:55:20Z-
dc.date.issued1998-
dc.identifier.issn0916-8451-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4391-
dc.description.abstractThe gene coding for an extracellular lipase of Bacillus stearothermophilus L1 was cloned in Escherichia coli. Sequence analysis showed an open reading frame of 1254 bp, which encodes a polypeptide of 417 amino acid residues. The polypeptide was composed of a signal sequence (29 amino acids) and a mature protein of 388 amino acids. An alanine replaces the first glycine in the conserved pentapeptide (Gly-X-Ser-X-Gly) around the active site serine. The expressed lipase was purified by hydrophobic interaction and ion exchange chromatography using buffers containing 0.02% (v/v) Triton X-100. The lipase was most active at 60-65°C and in alkaline conditions around pH 9-10. The lipase had highest activity toward p-nitrophenyl caprylate among the synthetic substrates and tripropionin among the triglycerides. It hydrolyzed beef tallow and palm oil more rapidly than olive oil at 50°C.-
dc.publisherT&F (Taylor & Francis)-
dc.titleGene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1-
dc.title.alternativeGene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1-
dc.typeArticle-
dc.citation.titleBioscience Biotechnology and Biochemistry-
dc.citation.number1-
dc.citation.endPage71-
dc.citation.startPage66-
dc.citation.volume62-
dc.contributor.affiliatedAuthorHyung Kwoun Kim-
dc.contributor.affiliatedAuthorSun Yang Park-
dc.contributor.affiliatedAuthorJung Kee Lee-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.alternativeName김형권-
dc.contributor.alternativeName박순양-
dc.contributor.alternativeName이정기-
dc.contributor.alternativeName오태광-
dc.identifier.bibliographicCitationBioscience Biotechnology and Biochemistry, vol. 62, no. 1, pp. 66-71-
dc.identifier.doi10.1271/bbb.62.66-
dc.subject.keywordlipase-
dc.subject.keywordBacillus stearothermophilus-
dc.subject.keywordthermostable enzyme-
dc.subject.locallipase-
dc.subject.localLipase-
dc.subject.localBacillus stearothermophilus-
dc.subject.localbacillus stearothermophilus-
dc.subject.localthermostable enzyme-
dc.subject.localThermostable enzyme-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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