Stability and catalytic properties of penicillin acylase in systems with low water content.
Stability and catalytic properties of native and immobilized penicillin acylase were studied in systems with low water content. Preparations of both native and immobilized penicillin acylase demonstrated the catalytic activity even in solid-phase systems which contained 3-5 wt. % of water. The stability and catalytic activity of penicillin acylase at low water content depended on the thermodynamic water activity (aw) in the system.
Youshko
M I
MI
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119899, Russia.
Sinev
A V
AV
Svedas
V K
VK
D002384:Catalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism; D010399:Penicillin Amidase / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D004800:Enzymes, Immobilized; D014867:Water; D010399:Penicillin Amidase