文献类型： 会议论文

第一作者： Bo Chen

作者： Bo Chen ¹ ; Richard A Gross ² ; M Elizabeth Miller;

作者机构： 1.NSF I/UCRC for Biocatalysis and Bioprocessing of Macromolecules, Polytechnic University, 6 Metrotech Center, Brooklyn, NY 11201

2.Rohm and Haas Co. P.O. Box 904, Spring House PA 19477

会议名称： PMSE PREPRINTS

主办单位：

页码： 1-2

摘要： Due to its unique properties Candida antarctica lipase B (CAL-B) is attracting increased attention as a biocatalyst for chemical synthesis. The enzyme exhibits a high degree of selectivity and a very broad substrate specificity1. The immobilization of enzymes via adsorption is a method well known for its ability to enhance enzyme stability, permit enzyme recyclability and therefore has been useful in efforts to develop new biocatalysts2. There are numerous publications for the synthesis of less complex structures and for polymerization reactions using immobilized CAL-B. Almost all publications on CAL-B use the commercially available catalyst marketed as Novozyme 435, which consists of CAL-B physically immobilized onto a macroporous acrylic polymer resin (Lewatit VP OC 1600, Bayer).

分类号： O63