Adsorption and Activity of Lipase on Polyphosphazene-Modified Polypropylene Membrane Surface

In this work, poly(n-butylamino)(allylamino)phosphazene (PBAP) was synthesized and tethered on polypropylene microporous membrane (PPMM) with the aim of offering a biocompatible and, at the same time, moderately hydrophobic microenvironment to lipase for the first time. Lipase from Candida rugosa wa...

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Bibliographic Details
Published in:Catalysts 2016-11, Vol.6 (11), p.174-174
Main Authors: Chen, Peng-Cheng, Qian, Yue-Cheng, Fang, Fei, Zhu, Xue-Yan, Huang, Xiao-Jun
Format: Article
Language:English
Subjects:
activity
Adsorption
Candida rugosa
Catalysts
Chemical reactions
Lipase
membrane modification
Membranes
polyphosphazene
Polypropylenes
Stability
Surface chemistry
Synthesis
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Summary:In this work, poly(n-butylamino)(allylamino)phosphazene (PBAP) was synthesized and tethered on polypropylene microporous membrane (PPMM) with the aim of offering a biocompatible and, at the same time, moderately hydrophobic microenvironment to lipase for the first time. Lipase from Candida rugosa was used and the influence of membrane surface conditions on the activities of immobilized lipases was evaluated. Water contact angle measurement as well as field emission scanning electron microscopy were used to characterize the morphology of the modified membranes. The results showed an improvement in the adsorption capacity (26.0 mg/m2) and activity retention (68.2%) of the immobilized lipases on the PBAP-modified PPMM. Moreover, the lipases immobilized on the modified PPMM showed better thermal and pH stability.
ISSN:2073-4344
2073-4344
DOI:10.3390/catal6110174