TY - JOUR
T1 - Construction of an immobilized thermophilic esterase on epoxy support for poly(ϵ-caprolactone) synthesis
AU - Ren, Hui
AU - Xing, Zhen
AU - Yang, Jiebing
AU - Jiang, Wei
AU - Zhang, Gang
AU - Tang, Jun
AU - Li, Quanshun
N1 - Publisher Copyright:
© 2016 by the authors; licensee MDPI.
Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 2016/6/1
Y1 - 2016/6/1
N2 - Developing an efficient immobilized enzyme is of great significance for improving the operational stability of enzymes in poly(ϵ-caprolactone) synthesis. In this paper, a thermophilic esterase AFEST from the archaeon Archaeoglobus fulgidus was successfully immobilized on the epoxy support Sepabeads EC-EP via covalent attachment, and the immobilized enzyme was then employed as a biocatalyst for poly(ϵ-caprolactone) synthesis. The enzyme loading and recovered activity of immobilized enzyme was measured to be 72 mg/g and 10.4 U/mg using p-nitrophenyl caprylate as the substrate at 80°C, respectively. Through the optimization of reaction conditions (enzyme concentration, temperature, reaction time and medium), poly(ϵ-caprolactone) was obtained with 100% monomer conversion and low number-average molecular weight (Mn < 1300 g/mol). Further, the immobilized enzyme exhibited excellent reusability, with monomer conversion values exceeding 75% during 15 batch reactions. Finally, poly(ϵ-caprolactone) was enzymatically synthesized with an isolated yield of 75% and Mn value of 3005 g/mol in a gram-scale reaction.
AB - Developing an efficient immobilized enzyme is of great significance for improving the operational stability of enzymes in poly(ϵ-caprolactone) synthesis. In this paper, a thermophilic esterase AFEST from the archaeon Archaeoglobus fulgidus was successfully immobilized on the epoxy support Sepabeads EC-EP via covalent attachment, and the immobilized enzyme was then employed as a biocatalyst for poly(ϵ-caprolactone) synthesis. The enzyme loading and recovered activity of immobilized enzyme was measured to be 72 mg/g and 10.4 U/mg using p-nitrophenyl caprylate as the substrate at 80°C, respectively. Through the optimization of reaction conditions (enzyme concentration, temperature, reaction time and medium), poly(ϵ-caprolactone) was obtained with 100% monomer conversion and low number-average molecular weight (Mn < 1300 g/mol). Further, the immobilized enzyme exhibited excellent reusability, with monomer conversion values exceeding 75% during 15 batch reactions. Finally, poly(ϵ-caprolactone) was enzymatically synthesized with an isolated yield of 75% and Mn value of 3005 g/mol in a gram-scale reaction.
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U2 - 10.3390/molecules21060796
DO - 10.3390/molecules21060796
M3 - Article
C2 - 27322233
AN - SCOPUS:84976406221
VL - 21
JO - Molecules
JF - Molecules
SN - 1420-3049
IS - 6
M1 - 796
ER -