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Biocatalytic production of lactose ester catalysed by mica-based immobilised lipase

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dc.Chemicals/CASmica, 12001-26-2; triacylglycerol lipase, 9001-62-1
dc.FundingDetailsFakulti Pertanian, Universiti Putra Malaysia Ministry of Higher Education, Malaysia,�MOHE
dc.FundingDetailsThis project was financially supported by research grants from Genetics and Molecular Biology Initiative , Ministry of Higher Education (MOHE), Malaysia and Universiti Putra Malaysia (UPM) .
dc.citedby32
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.authorAbdul Rahman M.B.en_US
dc.contributor.authorOthman S.S.en_US
dc.contributor.authorBasri M.en_US
dc.contributor.authorAbdulmalek E.en_US
dc.contributor.authorAbdul Rahman R.N.Z.R.en_US
dc.contributor.authorSalleh A.B.en_US
dc.date.accessioned2024-05-29T01:59:47Z
dc.date.available2024-05-29T01:59:47Z
dc.date.issued2012
dc.description.abstractEnzyme immobilisation technology is an effective means to improve sugar ester production through the employment of biocatalysts. In the present study, immobilisation of Candida rugosa (CRL) lipase onto amino-activated mica is performed via covalent bonding (namely Amino-CRL) and the cross-linking of lipases into nano-reactors through physical adsorption (namely NER-CRL). Free and immobilised lipases were tested for their esterification activities. Specific activities for Amino-CRL and NER-CRL increased by 2.4 and 2.6-fold, respectively, upon immobilisation. Extending this work, immobilised lipases have novel capabilities in the synthesis of sugar esters. The optimised conditions for sugar fatty acid ester syntheses are 48 h at 2:1 of molar ratio of lactose sugar to capric acid at 55 �C. Furthermore, a high operational stability with half-lives of over 13 and 10 runs was achieved for NER-CRL and Amino-CRL, respectively, indicating the efficiency of the immobilisation process. � 2011 Elsevier Ltd. All rights reserved.en_US
dc.description.natureFinalen_US
dc.identifier.CODENFOCHD
dc.identifier.doi10.1016/j.foodchem.2011.08.060
dc.identifier.epage205
dc.identifier.issn3088146
dc.identifier.issue1
dc.identifier.scopus2-s2.0-80054024932
dc.identifier.spage199
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-80054024932&doi=10.1016%2fj.foodchem.2011.08.060&partnerID=40&md5=74d5086cd6c9f9fe0644e23bd97d49e3
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/10083
dc.identifier.volume131
dc.languageEnglish
dc.language.isoen_USen_US
dc.relation.ispartofFood Chemistry
dc.sourceScopus
dc.subjectCandida rugosa lipaseen_US
dc.subjectCovalent bondingen_US
dc.subjectCross-linkingen_US
dc.subjectMicaen_US
dc.subjectSugar estersen_US
dc.titleBiocatalytic production of lactose ester catalysed by mica-based immobilised lipaseen_US
dc.title.alternativeFood Chem.en_US
dc.typeArticleen_US
dspace.entity.typePublication

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