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標題: Effect of membranes with various hydrophobic/hydrophilic properties on lipase immobilized activity and stability
作者: Chen, G.J.
Kuo, C.H.
Chen, C.I.
Yu, C.C.
Shieh, C.J.
Liu, Y.C.
關鍵字: Lipase;Covalent immobilization;Polyvinylidene fluoride;Hydrophobicity;Surface modification;metal affinity membranes;covalent immobilization;candida-rugosa;purification;chitosan;chromatography;enhancement;hydrolysis;adsorption
Project: Journal of Bioscience and Bioengineering
期刊/報告no:: Journal of Bioscience and Bioengineering, Volume 113, Issue 2, Page(s) 166-172.
In 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.
ISSN: 1389-1723
DOI: 10.1016/j.jbiosc.2011.09.023
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