Application of ring-opening metathesis polymerization in study of polymer molecular weight-mediated catalytic properties of immobilized lipase |
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Authors: | Chuang Du Guo Zhang Zhi Wang Lei Li Jun Tang Lei Wang |
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Institution: | (1) College of Chemistry, Alan G. MacDiarmid Institute, Jilin University, Changchun, 130023, China;(2) Key Laboratory of Excited State Physics, Changchun Institute of Optics, Fine Mechanics and Physics, Chinese Academy of Sciences, Changchun, 130033, China;(3) Key Laboratory of Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun, 130023, China |
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Abstract: | Recently, significant efforts have been devoted into the study of the effect of hydrophobic supports on the catalytic properties
of immobilized lipases. It seems that immobilization lipases on hydrophobic supports is a simple and efficient method to improve
the catalytic activity of lipases. In this study, the hydrophobic poly(N-propyl-norbornene-exo-2,3-dicarboximide)s with well-controlled
molecular weight were synthesized by the living ring-opening metathesis polymerization, and the lipases from Pseudomonas sp. were then immobilized on these hydrophobic polymer supports through the physical adsorption. The immobilized lipases exhibited
higher activity and enantioselectivity for the transesterification of 2-octanol than those of free lipases. Furthermore, we
investigated the polymer molecular weight-mediated catalytic properties of immobilized lipases. It was found that the catalytic
activity and E value of the immobilized lipases increased with the increase of the polymer molecular weight. At the polymeric molecular
weight of about 40kDa, the highest E value (58 at 54.2% of conversion, enantiomeric excess = 99%) was reached. After the molecular weight of polymers getting
higher than 40 kDa, catalytic activity and E value of the immobilized lipase decreased.
Supported by the Stake Key Development Program of Basic Research of China (Grant No.2007CB808000) and National Natural Science
Foundation of China (Grant Nos. 50773028, and 20803028). |
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Keywords: | ring-opening metathesis polymerization interface lipase |
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