Document Detail


Lipase-catalyzed synthesis and characterization of polymers by cyclodextrin as support architecture.
MedLine Citation:
PMID:  23218346     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Diesters and diols were successfully converted into aliphatic polyesters by enzymatic lipase Candida sp.99-125 catalysis, with β-cyclodextrin acting as supporting architecture (in a similar way as chaperone proteins). No organic solvents were used. The polytransesterification was a much greener process, being solvent-free and without metal residues. Lipase Candida sp.99-125 showed a high catalytic activity for bulkpolymerization of diesters and diols with various numbers of methylene groups in their chains. β-Cyclodextrin encircled the linear polymer chain and maintained the chain in a proper configuration to avoid its coagulation. Lipase initiated the polymerization and β-cyclodextrin threaded onto the polymer chain to control the structure for producing high molecular weight polyesters. From a combination of diesters and diols, polyesters with a high molecular weight of 62,100Da were obtained at 70°C. The corresponding polyesters showed an excellent thermal stability till 350°C and had a strong ability to crystallize with up to 72% crystallinity, contributing to their high storage modulus.
Authors:
Wenhui Liu; Fang Wang; Tianwei Tan; Biqiang Chen
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Publication Detail:
Type:  Journal Article     Date:  2012-10-02
Journal Detail:
Title:  Carbohydrate polymers     Volume:  92     ISSN:  1879-1344     ISO Abbreviation:  Carbohydr Polym     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-10     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8307156     Medline TA:  Carbohydr Polym     Country:  England    
Other Details:
Languages:  eng     Pagination:  633-40     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ltd. All rights reserved.
Affiliation:
The Biorefinery Research and Engineering Center of the Ministry of Education, Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China.
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