Purification and characterization of acidic lipase from Aspergillus niger NCIM 1207

被引：101
|
作者：
Mhetras, N. C. [1 ]
Bastawde, K. B. [1 ]
Gokhale, D. V. [1 ]
机构：
[1] Natl Chem Lab, NCIM Resource Ctr, Pune 411008, Maharashtra, India
来源：
BIORESOURCE TECHNOLOGY | 2009年 / 100卷 / 03期
关键词：
Acidic lipase; Aspergillus niger; Positional specificity; EXTRACELLULAR LIPASE; IDENTIFICATION; RESIDUES;
D O I：
10.1016/j.biortech.2008.08.016
中图分类号：
S2 [农业工程];
学科分类号：
0828 ;
摘要：
An extracellular lipase from Aspergillus niger NCIM 1207 has been purified to homogeneity using ammonium sulfate precipitation followed by phenyl sepharose and Sephacryl-100 gel chromatography. This protocol resulted in 149 fold purification with 54% final recovery. The purified enzyme showed a prominent single band on SDS-PAGE. The purified enzyme is a monomeric protein of 32.2 kDa molecular weight and exhibits optimal activity at 50 degrees C. One interesting feature of this enzyme is its highly acidic pH optimum. The isoelectric point (pl) of lipase was 8.5. The purified lipase appears to be unique since it cleaved triolein at only 3-position releasing 1,2-diolein. Chemical modification studies revealed that His, Ser, Carboxylate and Trp are involved in catalysis. (c) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码：1486 / 1490
页数：5
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