Sweet polyesters: Lipase-catalyzed condensation - Polymerizations of alditols

被引:56
|
作者
Hu, Jun [1 ]
Gao, Wei [1 ]
Kulshrestha, Ankur [1 ]
Gross, Richard A. [1 ]
机构
[1] Polytech Univ, Dept Chem & Biol Sci, Metrotech Ctr 6, NSFI UCRC Biocatalysis & Bioproc Macromol, Brooklyn, NY 11201 USA
关键词
D O I
10.1021/ma0612834
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
The use of isolated enzymes of lipase as catalyst in the preparation of both functional linear polymers and polymers with improved control over branching for polymerization reactions is discussed. Lipases are well established catalysts for regioselective esterification of low molar mass substrates at mild temperature. Lipase regioselectivity can be varied by many parameters that includes substrate structure, lipase structure, lipase immobilization, reaction medium, time , and temperature. The expanded set of naturally derived polyols was accessed for their potential to form high molecular weight polyol-polysters by N435 catalysis. The importance of precise vacuum control on reproducibility of experiments was established. Th results show that the expanded set of polylols and reproducible reaction conditions illucidate the details of regioselectivity and branching during enzyme-catalyzed polyol-polyster polymerization.
引用
收藏
页码:6789 / 6792
页数:4
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