Purification and biochemical properties of microbial pectinases - a review

被引:180
|
作者
Gummadi, SN [1 ]
Panda, T [1 ]
机构
[1] Indian Inst Technol, Dept Chem Engn, Biotechnol Res Ctr, Madras 600036, Tamil Nadu, India
关键词
microbial pectinases; applications; purification; stability; hydrolysis; chemical modification;
D O I
10.1016/S0032-9592(02)00203-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Pectinases are a complex group of enzymes that degrade various pectic substances present in plant tissues. Pectinases have potential applications in fruit, paper and textile industries. Apart from these industrial applications, these enzymes possess biological importance in protoplast fusion technology and plant pathology. Since applications of pectinases in various fields are widening, it is important to understand the nature and properties of these enzymes for efficient and effective usage. For the past few years, vigorous research has been carried out on isolation and characterization of pectinases. New affinity matrices with improved characteristics and affinity-precipitation techniques have been developed for purification of pectinases. Recently much attention has been focused on chemical modification of pectinases and their catalytic performance by various researchers. These studies are helpful in determining key amino acid residues responsible for substrate binding, catalytic action, and physico-chemical environmental conditions for maximum hydrolysis. This short review highlights progress on purification and understanding the biochemical aspects of microbial pectinases. (C) 2002 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:987 / 996
页数:10
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