Purification and characterization of an alkaline lipase from a newly isolated Acinetobacter radioresistens CMC-1

被引：24
|
作者：
Hong, MC [1 ]
Chang, MC [1 ]
机构：
[1] Natl Cheng Kung Univ, Coll Med, Dept Biochem, Tainan 70101, Taiwan
来源：
BIOTECHNOLOGY LETTERS | 1998年 / 20卷 / 11期
关键词：
D O I：
10.1023/A:1005407005371
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
A novel alkaline lipase showing a broad range of specificity towards long chain triacylglycerols or p-nitrophenyl esters was purified to homogeneity from Acinetobacter radioresistens CMC-1. Its molecular mass was 45 kDa (by SDS-PAGE), pi of approx. 5.2, and optimally activity at 10.5 and 40 degrees C. Using triolein as substrate, the lipase showed 1,3-positional specificity for hydrolyzing ester bonds. The enzyme was activated in 40% (v/v) dimethylsulfoxide and 20% (v/v) dimethylformamide.
引用
收藏
页码：1027 / 1029
页数：3
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