THERMOPHILIC LIPASE AND RECOMBINANT ESCHERICHIA COLI WHOLE-CELL:NOVEL BIOCATALYSTS FOR THE SYNTHESIS OF BIODEGRADABLE POLYESTERS

摘要：

In this paper we have explored the catalytic activity of a novel thermophilic lipase FNL from Fervidobacterium nodosum for biodegradable polyester synthesis, using the ring-opening polymerization of ε-caprolactone as the model. Through the optimization of reaction conditions, poly(ε-caprolactone) was obtained with almost 100％ monomer conversion, with a number-average molecular weight (Mn) of 2340 g/mol and a polydispersity index (PDI) of 1.34. Michaelis-Menten kinetic analysis showed that the enzyme had a high affinity for ε-caprolactone with a Km value of 0.35 mol/L. The possible structural and energy aspects of the interaction of enzyme and the monomer ε-caprolactone were elucidated using molecular docking. Furthermore, as the enzyme was expressed in an active insoluble form, the recombinant E. coli whole-cell exhibited excellent catalytic activity and operational stability.

关键词： poly(ε-caprolactone) thermophilic lipase whole-cell biocatalyst kinetic analysis molecular docking

作者: Quanshun Li Gaungquan Li Wei Shi

作者单位: Key Laboratory for Molecular Enzymology and Engineering, the Ministry of Education, Jilin University Key Laboratory for Molecular Enzymology and Engineering, the Ministry of Education, Jilin University

会议类型: 国际会议

会议名称: The First Symposium on Innovative Polymers for Controlled Delivery(新型高分子材料与控制释放国际会议 SIPCD 2010)

会议地点: 苏州

会议语种:英文

页码: 505-507

在线出版日期: 2010-09-14（万方平台首次上网日期，不代表论文的发表时间）