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Int. J. Mol. Sci. 2012, 13(10), 12232-12241; doi:10.3390/ijms131012232

Biocatalytic Synthesis of Poly(δ-Valerolactone) Using a Thermophilic Esterase from Archaeoglobus fulgidus as Catalyst

1,* , 2,*  and 1,*
1 Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, Changchun 130012, China 2 Department of General Surgery, Second Hospital, Jilin University, Changchun 130041, China These authors contributed equally to this work.
* Authors to whom correspondence should be addressed.
Received: 26 July 2012 / Revised: 24 August 2012 / Accepted: 7 September 2012 / Published: 25 September 2012
(This article belongs to the Special Issue Enzyme Optimization and Immobilization)
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The ring-opening polymerization of δ-valerolactone catalyzed by a thermophilic esterase from the archaeon Archaeoglobus fulgidus was successfully conducted in organic solvents. The effects of enzyme concentration, temperature, reaction time and reaction medium on monomer conversion and product molecular weight were systematically evaluated. Through the optimization of reaction conditions, poly(δ-valerolactone) was produced in 97% monomer conversion, with a number-average molecular weight of 2225 g/mol, in toluene at 70 °C for 72 h. This paper has produced a new biocatalyst for the synthesis of poly(δ-valerolactone), and also deeper insight has been gained into the mechanism of thermophilic esterase-catalyzed ring-opening polymerization.
Keywords: thermophilic esterase; ring-opening polymerization; δ-valerolactone thermophilic esterase; ring-opening polymerization; δ-valerolactone
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Cao, H.; Han, H.; Li, G.; Yang, J.; Zhang, L.; Yang, Y.; Fang, X.; Li, Q. Biocatalytic Synthesis of Poly(δ-Valerolactone) Using a Thermophilic Esterase from Archaeoglobus fulgidus as Catalyst. Int. J. Mol. Sci. 2012, 13, 12232-12241.

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