Activity of penicillin acylase from E. coli in the reversed-micelle system AOT--H2O--octane.
The behavior of a penicillin acylase from E. coli was studied in the reversed-micelle system AOT--H2O--octane. Kinetic studies of the enzymatic hydrolysis of the m-carboxy-p-nitroanilide of phenylacetic acid, titration of the penicillin acylase active site with an irreversible specific inhibitor (phenylmethylsulfonyl fluoride), sedimentation analysis at different hydration degrees, and chemical modification showed that the enzyme loses no more than 20% of its initial activity during 3-4 h in the reversed-micelle systems of different hydration degrees and retains its catalytically active structure.
Shamolina
T A
TA
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia.
Drachev
V A
VA
Svedas
V K
VK
D002384:Catalysis; D004143:Dioctyl Sulfosuccinic Acid; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D008823:Micelles; D009795:Octanes; D010399:Penicillin Amidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D014867:Water
D004791:Enzyme Inhibitors; D008823:Micelles; D009795:Octanes; D014867:Water; D004143:Dioctyl Sulfosuccinic Acid; D010664:Phenylmethylsulfonyl Fluoride; D010399:Penicillin Amidase; C026728:octane