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Physical and Covalent Immobilization of Lipase onto Amine Groups Bearing Thiol-Ene Photocured Coatings

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dc.contributor.authorÇAKMAKÇI, EMRAH
dc.contributor.authorsCakmakci, Emrah; Muhsir, Pelin; Demir, Serap
dc.date.accessioned2022-03-12T20:31:12Z
dc.date.available2022-03-12T20:31:12Z
dc.date.issued2017
dc.description.abstractIn this study, amine groups containing thiol-ene photocurable coating material for lipase immobilization were prepared. Lipase (EC 3.1.1.3) from Candida rugosa was immobilized onto the photocured coatings by physical adsorption and glutaraldehyde-activated covalent bonding methods, respectively. The catalytic efficiency of the immobilized and free enzymes was determined for the hydrolysis of p-nitrophenyl palmitate and also for the synthesis of p-nitrophenyl linoleate. The storage stability and the reusability of the immobilized enzyme and the effect of temperature and pH on the catalytic activities were also investigated. The optimum pH for free lipase and physically immobilized lipase was determined as 7.0, while it was found as 7.5 for the covalent immobilization. After immobilization, the optimum temperature increased from 37 A degrees C (free lipase) to 50-55 A degrees C. In the end of 15 repeated cycles, covalently bounded enzyme retained 60 and 70 % of its initial activities for hydrolytic and synthetic assays, respectively. While the physically bounded enzyme retained only 56 % of its hydrolytic activity and 67 % of its synthetic activity in the same cycle period. In the case of hydrolysis V (max) values slightly decreased after immobilization. For synthetic assay, the V (max) value for the covalently immobilized lipase was found as same as free lipase while it decreased dramatically for the physically immobilized lipase. Physically immobilized enzyme was found to be superior over covalent bonding in terms of enzyme loading capacity and optimum temperature and exhibited comparable re-use values and storage stability. Thus, a fast, easy, and less laborious method for lipase immobilization was developed.
dc.identifier.doi10.1007/s12010-016-2266-6
dc.identifier.eissn1559-0291
dc.identifier.issn0273-2289
dc.identifier.pubmed27704477
dc.identifier.urihttps://hdl.handle.net/11424/234261
dc.identifier.wosWOS:000394992900012
dc.language.isoeng
dc.publisherHUMANA PRESS INC
dc.relation.ispartofAPPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectLipase
dc.subjectThiol-ene
dc.subjectCovalent immobilization
dc.subjectPhysical adsorption
dc.subjectPhotocuring
dc.subjectCANDIDA-RUGOSA LIPASE
dc.subjectALPHA-AMYLASE
dc.subjectENZYME IMMOBILIZATION
dc.subjectCHEMICAL-MODIFICATION
dc.subjectCROSS-LINKING
dc.subjectGLUTARALDEHYDE
dc.subjectSTABILITY
dc.subjectMEMBRANE
dc.subjectSUPPORTS
dc.subjectPURIFICATION
dc.titlePhysical and Covalent Immobilization of Lipase onto Amine Groups Bearing Thiol-Ene Photocured Coatings
dc.typearticle
dspace.entity.typePublication
local.avesis.ida7f4d581-1d06-47cf-bd41-d04c3db41350
local.import.packageSS17
local.indexed.atWOS
local.indexed.atSCOPUS
local.indexed.atPUBMED
local.journal.numberofpages18
local.journal.quartileQ3
oaire.citation.endPage1047
oaire.citation.issue3
oaire.citation.startPage1030
oaire.citation.titleAPPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
oaire.citation.volume181
relation.isAuthorOfPublication332869cd-e8a9-40ac-b678-cf5b01c6a6dc
relation.isAuthorOfPublication.latestForDiscovery332869cd-e8a9-40ac-b678-cf5b01c6a6dc

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