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Effect of membranes with various hydrophobic/hydrophilic properties on lipase immobilized activity and stability

Paper ID Volume ID Publish Year Pages File Format Full-Text
21371 43219 2012 7 PDF Available
Title
Effect of membranes with various hydrophobic/hydrophilic properties on lipase immobilized activity and stability
Abstract

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.

Keywords
Al/Am, alkyl/amine tail ratio; BA, n-butylamine; CC, cyanuric chloride; DA, 1,4-diaminobutane; EPI, epichlorohydrin; GA, glutaraldehyde; GF, glass fiber; H/H, hydrophobic/hydrophilic; I/F, immobilization/free; PVDF, polyvinylidene fluoride; RC, regenerate
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Effect of membranes with various hydrophobic/hydrophilic properties on lipase immobilized activity and stability
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 113, Issue 2, February 2012, Pages 166–172
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us