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Kinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar esters

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dc.Chemicals/CASaluminum silicate, 12183-80-1, 1302-93-8, 1318-74-7, 1335-30-4, 61027-90-5; decanoic acid, 334-48-5, 3398-75-2; lactose, 10039-26-6, 16984-38-6, 63-42-3, 64044-51-5; mica, 12001-26-2; triacylglycerol lipase, 9001-62-1; Aluminum Silicates; Bacterial Proteins; Cross-Linking Reagents; Decanoic Acids; Enzymes, Immobilized; Esters; Lactose, 63-42-3; Lipase, 3.1.1.3; decanoic acid, 334-48-5; mica, 12001-26-2
dc.FundingDetailsUniversiti Putra Malaysia Ministry of Higher Education, Malaysia,�MOHE
dc.FundingDetailsThis project was financially supported by research grants from the Genetics and Molecular Biology Initiative of Ministry of Higher Education (MOHE) in Malaysia and by Universiti Putra Malaysia (UPM).
dc.citedby2
dc.contributor.affiliationsFaculty of Science and Technology
dc.contributor.affiliationsUniversiti Putra Malaysia (UPM)
dc.contributor.affiliationsMalaysia Genome Institute
dc.contributor.affiliationsUniversiti Sains Islam Malaysia (USIM)
dc.contributor.authorZaidan U.H.en_US
dc.contributor.authorRahman M.B.A.en_US
dc.contributor.authorOthman S.S.en_US
dc.contributor.authorBasri M.en_US
dc.contributor.authorAbdulmalek E.en_US
dc.contributor.authorRahman R.N.Z.R.A.en_US
dc.contributor.authorSalleh A.B.en_US
dc.date.accessioned2024-05-29T02:04:17Z
dc.date.available2024-05-29T02:04:17Z
dc.date.issued2011
dc.description.abstractThe utilization of natural mica as a biocatalyst support in kinetic investigations is first described in this study. The formation of lactose caprate from lactose sugar and capric acid, using free lipase (free-CRL) and lipase immobilized on nanoporous mica (NER-CRL) as a biocatalyst, was evaluated through a kinetic study. The apparent kinetic parameters, Km and Vmax, were determined by means of the Michaelis-Menten kinetic model. The Ping-Pong Bi-Bi mechanism with single substrate inhibition was adopted as it best explains the experimental findings. The kinetic results show lower Km values with NER-CRL than with free-CRL, indicating the higher affinity of NER-CRL towards both substrates at the maximum reaction velocity (Vmax,app > Vmax). The kinetic parameters deduced from this model were used to simulate reaction rate data which were in close agreement with the experimental values.en_US
dc.description.natureFinalen_US
dc.identifier.CODENBBBIE
dc.identifier.doi10.1271/bbb.110117
dc.identifier.epage1450
dc.identifier.issn9168451
dc.identifier.issue8
dc.identifier.pmid21821960
dc.identifier.scopus2-s2.0-80052020034
dc.identifier.spage1446
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-80052020034&doi=10.1271%2fbbb.110117&partnerID=40&md5=7ea0ac83f2963ae42fc517c48ccd5cb6
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/10289
dc.identifier.volume75
dc.languageEnglish
dc.language.isoen_USen_US
dc.relation.ispartofBioscience, Biotechnology and Biochemistryen_US
dc.sourceScopus
dc.subjectKinetic studyen_US
dc.subjectLipase immobilizationen_US
dc.subjectMicaen_US
dc.subjectPing-Pong Bi-Bi modelen_US
dc.subjectSugar ester synthesisen_US
dc.titleKinetic behaviour of free lipase and mica-based immobilized lipase catalyzing the synthesis of sugar estersen_US
dc.title.alternativeBiosci. Biotechnol. Biochem.en_US
dc.typeArticleen_US
dspace.entity.typePublication

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