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Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/14668
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dc.contributor.authorKanjanavas P.
dc.contributor.authorKhuchareontaworn S.
dc.contributor.authorKhawsak P.
dc.contributor.authorPakpitcharoen A.
dc.contributor.authorPothivejkul K.
dc.contributor.authorSantiwatanakul S.
dc.contributor.authorMatsui K.
dc.contributor.authorKajiwara T.
dc.contributor.authorChansiri K.
dc.date.accessioned2021-04-05T03:36:21Z-
dc.date.available2021-04-05T03:36:21Z-
dc.date.issued2010
dc.identifier.issn14220067
dc.identifier.other2-s2.0-77958115682
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/14668-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77958115682&doi=10.3390%2fijms11103783&partnerID=40&md5=908da2092b664a3914a05d0821f831db
dc.description.abstractThe aim of this study was to characterize the organic solvent and detergent tolerant properties of recombinant lipase isolated from thermotolerant Bacillus sp. RN2 (Lip-SBRN2). The isolation of the lipase-coding gene was achieved by the use of inverse and direct PCR. The complete DNA sequencing of the gene revealed that the lip-SBRN2 gene contains 576 nucleotides which corresponded to 192 deduced amino acids. The purified enzyme was homogeneous with the estimated molecular mass of 19 kDa as determined by SDS-PAGE and gel filtration. The Lip-SBRN2 was stable in a pH range of 9-11 and temperature range of 45-60 °C. The enzyme was a non metallo-monomeric protein and was active against pNP-caprylate (C8) and pNP-laurate (C12) and coconut oil. The Lip-SBRN2 exhibited a high level of activity in the presence of 108% benzene, 102.4% diethylether and 112% SDS. It is anticipated that the organic solvent and detergent tolerant enzyme secreted by Bacillus sp. RN2 will be applicable as catalysts for reaction in the presence of organic solvents and detergents. © 2010 by the authors; licensee MDPI.
dc.subject4 nitrophenyl caprylate
dc.subjectbacterial enzyme
dc.subjectbenzene
dc.subjectcoconut oil
dc.subjectdetergent
dc.subjectedetic acid
dc.subjectesterase inhibitor
dc.subjectether
dc.subjectlauric acid 4 nitrophenyl ester
dc.subjectlauric acid derivative
dc.subjectmetal ion
dc.subjectoctanoic acid
dc.subjectoctanoic acid derivative
dc.subjectorganic solvent
dc.subjectrecombinant enzyme
dc.subjectRN2 protein
dc.subjecttriacylglycerol lipase
dc.subjectunclassified drug
dc.subjectarticle
dc.subjectBacillus
dc.subjectbacterial strain
dc.subjectbiocatalyst
dc.subjectcontrolled study
dc.subjectDNA sequence
dc.subjectenzyme activity
dc.subjectenzyme analysis
dc.subjectenzyme isolation
dc.subjectenzyme purification
dc.subjectenzyme specificity
dc.subjectenzyme stability
dc.subjectgel filtration
dc.subjectgenetic code
dc.subjectheat tolerance
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectnucleotide sequence
dc.subjectpH measurement
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectpolymerase chain reaction
dc.subjectBacillus
dc.subjectdetergent tolerant
dc.subjectlipase
dc.subjectorganic tolerant
dc.subjectthermotolerant
dc.subjectBacillus
dc.subjectBacterial Proteins
dc.subjectDetergents
dc.subjectHot Temperature
dc.subjectLipase
dc.subjectSolvents
dc.subjectBacillus sp.
dc.subjectBacillus
dc.subjectdetergent tolerant
dc.subjectlipase
dc.subjectorganic tolerant
dc.subjectthermotolerant
dc.titlePurification and characterization of organic solvent and detergent tolerant lipase from thermotolerant Bacillus sp. RN2
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationInternational Journal of Molecular Sciences. Vol 11, No.10 (2010), p.3783-3792
dc.identifier.doi10.3390/ijms11103783
Appears in Collections:Scopus 1983-2021

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