Journal
MOLECULES
Volume 19, Issue 7, Pages 9838-9849Publisher
MDPI AG
DOI: 10.3390/molecules19079838
Keywords
immobilized enzyme; cross linking; thermophilic esterase; ring-opening polymerization; epsilon-caprolactone
Funding
- Natural Science Foundation of China [21204025, 81373344]
- Ministry of Science and Technology of China [2011DFR51090]
- Science & Technology Department of Jilin Province [20130522005JH, 20140101140JC]
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The immobilized thermophilic esterase from Archaeoglobus fulgidus was successfully constructed through the glutaraldehyde-mediated covalent coupling after its physical adsorption on a hydrophobic macroporous resin, Sepabeads EC-OD. Through 0.05% glutaraldehyde treatment, the prevention of enzyme leaching and the maintenance of catalytic activity could be simultaneously realized. Using the enzymatic ring-opening polymerization of e-caprolactone as a model, effects of organic solvents and reaction temperature on the monomer conversion and product molecular weight were systematically investigated. After the optimization of reaction conditions, products were obtained with 100% monomer conversion and M-n values lower than 1010 g/mol. Furthermore, the cross-linked immobilized thermophilic esterase exhibited an excellent operational stability, with monomer conversion values exceeding 90% over the course of 12 batch reactions, still more than 80% after 16 batch reactions.
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