Polymerization of Propyl Malolactonate in the Presence of Candida rugosa Lipase
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- 作者：Anna A. Panova ; Sonia Taktak ; Solo Randriamahefa ; Sandrine Cammas-Marion ; Philippe Guerin ; and David L. Kaplan
- 刊名：Biomacromolecules
- 出版年：2003
- 出版时间：January 2003
- 年：2003
- 卷：4
- 期：1
- 页码：19 - 27
- 全文大小：256K
- 年卷期：v.4,no.1(January 2003)
- ISSN：1526-4602
文摘
To gain better insight into mechanistic features of enzyme-catalyzed malolactonate polymerization, reactionswith propyl malolactonate were analyzed while varying enzyme concentration, reaction media composition,and reaction temperature. Monomer conversion and product molecular weights were characterized by 1HNMR and MALDI-TOF MS, respectively. A high extent of thermal polymerization of propyl malolactonatewas observed, while the polymer chain length in all reactions was controlled by the elimination of 
-hydrogenfrom propyl malolactonate with formation of a new initiator and the new chains. The most efficient enzymaticcatalysis occurred in toluene (2.11 M monomer) at 60 
C. Candida rugosa lipase (10 wt %) acceleratedpolymerization 25-fold over the rate of thermal polymerization. The maximum poly(propyl malate) number-average molecular weight obtained was 5000 Da at 20 wt % enzyme with a polydispersity of 1.15. Thesevalues compare with 1800 Da and 1.5, respectively, in the absence of enzyme.
-hydrogenfrom propyl malolactonate with formation of a new initiator and the new chains. The most efficient enzymaticcatalysis occurred in toluene (2.11 M monomer) at 60 C. Candida rugosa lipase (10 wt %) acceleratedpolymerization 25-fold over the rate of thermal polymerization. The maximum poly(propyl malate) number-average molecular weight obtained was 5000 Da at 20 wt % enzyme with a polydispersity of 1.15. Thesevalues compare with 1800 Da and 1.5, respectively, in the absence of enzyme.