THE USE OF PRESSURE TO MODIFY ENZYME-ACTIVITY IN REVERSED MICELLES

被引：8
|
作者：
RAO, AM [1 ]
KOMMAREDDI, N [1 ]
JOHN, VT [1 ]
机构：
[1] TULANE UNIV,DEPT CHEM ENGN,NEW ORLEANS,LA 70118
来源：
BIOTECHNOLOGY PROGRESS | 1992年 / 8卷 / 06期
关键词：
D O I：
10.1021/bp00018a007
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：
Pressurization of enzyme-containing AOT-water-isooctane reversed micelles with low molecular weight gases leads to markedly different responses in activity characteristics. Microbial lipases exhibit a total cutoff in activity with as low a pressure as 2 Wa and a remarkable activity regain with depressurization. The observation also holds for reaction in monophasic organic solvents. The protease, alpha-chymotrypsin, is unaffected by pressurization until a critical pressure wherein micellar instability occurs. The use of pressure as a switch for lipase reaction in nonaqueous media is discussed.
引用
收藏
页码：514 / 520
页数：7
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