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Molecules 2015, 20(5), 9358-9379; doi:10.3390/molecules20059358

Green Polymer Chemistry: Enzyme Catalysis for Polymer Functionalization

Department of Chemical and Biomolecular Engineering, The University of Akron, Akron, OH 44325, USA
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Author to whom correspondence should be addressed.
Academic Editor: Lajos Novak
Received: 11 April 2015 / Accepted: 15 May 2015 / Published: 21 May 2015
(This article belongs to the Special Issue Enzyme-Catalyzed Reactions)

Abstract

Enzyme catalyzed reactions are green alternative approaches to functionalize polymers compared to conventional methods. This technique is especially advantageous due to the high selectivity, high efficiency, milder reaction conditions, and recyclability of enzymes. Selected reactions can be conducted under solventless conditions without the application of metal catalysts. Hence this process is becoming more recognized in the arena of biomedical applications, as the toxicity created by solvents and metal catalyst residues can be completely avoided. In this review we will discuss fundamental aspects of chemical reactions biocatalyzed by Candida antarctica lipase B, and their application to create new functionalized polymers, including the regio- and chemoselectivity of the reactions. View Full-Text
Keywords: enzyme catalysis; Candida antarctica lipase B; transesterification; Michael addition; polymer functionalization,; poly(ethylene glycol); polyisobutylene; polysiloxanes; polystyrene; regioselectivity; chemoselectivity enzyme catalysis; Candida antarctica lipase B; transesterification; Michael addition; polymer functionalization,; poly(ethylene glycol); polyisobutylene; polysiloxanes; polystyrene; regioselectivity; chemoselectivity
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Sen, S.; Puskas, J.E. Green Polymer Chemistry: Enzyme Catalysis for Polymer Functionalization. Molecules 2015, 20, 9358-9379.

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