Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/69779
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dc.contributor.authorChen, G.J.en_US
dc.contributor.authorKuo, C.H.en_US
dc.contributor.authorChen, C.I.en_US
dc.contributor.authorYu, C.C.en_US
dc.contributor.authorShieh, C.J.en_US
dc.contributor.authorLiu, Y.C.en_US
dc.date2012zh_TW
dc.date.accessioned2014-06-11T05:58:53Z-
dc.date.available2014-06-11T05:58:53Z-
dc.identifier.issn1389-1723zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/69779-
dc.description.abstractIn this study, three membranes: regenerated cellulose (RC), glass fiber (GF) and polyvinylidene fluoride (PVDF), were grafted with 1,4-diaminobutane (DA) and activated with glutaraldehyde (GA) for lipase covalent immobilization. The efficiencies of lipases immobilized on these membranes with different hydrophobic/hydrophilic properties were compared. The lipase immobilized on hydrophobic PVDF-DA-GA membrane exhibited more than an 11-fold increase in activity compared to its immobilization on a hydrophilic RC-DA-GA membrane. The relationship between surface hydrophobicity and immobilized efficiencies was investigated using hydrophobic/hydrophilic GF membranes which were prepared by grafting a different ratio of n-butylamine/1,4-diaminobutane (BA/DA). The immobilized lipase activity on the GF membrane increased with the increased BA/DA ratio. This means that lipase activity was exhibited more on the hydrophobic surface. Moreover, the modified PVDF-DA membrane was grafted with GA, epichlorohydrin (EPI) and cyanuric chloride (CC), respectively. The lipase immobilized on the PVDF-DA-EPI membrane displayed the highest specific activity compared to other membranes. This immobilized lipase exhibited more significant stability on pH, thermal, reuse, and storage than did the free enzyme. The results exhibited that the EPI modified PVDF is a promising support for lipase immobilization. (C) 2011, The Society for Biotechnology, Japan. All rights reserved.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of Bioscience and Bioengineeringen_US
dc.relation.ispartofseriesJournal of Bioscience and Bioengineering, Volume 113, Issue 2, Page(s) 166-172.en_US
dc.relation.urihttp://dx.doi.org/10.1016/j.jbiosc.2011.09.023en_US
dc.subjectLipaseen_US
dc.subjectCovalent immobilizationen_US
dc.subjectPolyvinylidene fluorideen_US
dc.subjectHydrophobicityen_US
dc.subjectSurface modificationen_US
dc.subjectmetal affinity membranesen_US
dc.subjectcovalent immobilizationen_US
dc.subjectcandida-rugosaen_US
dc.subjectpurificationen_US
dc.subjectchitosanen_US
dc.subjectchromatographyen_US
dc.subjectenhancementen_US
dc.subjecthydrolysisen_US
dc.subjectadsorptionen_US
dc.titleEffect of membranes with various hydrophobic/hydrophilic properties on lipase immobilized activity and stabilityen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1016/j.jbiosc.2011.09.023zh_TW
item.languageiso639-1en_US-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextno fulltext-
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