[Properties of acylase preparations from an actinomycete culture].
A comparative study of some physico-chemical properties of high-purified preparations of extracellular penicillin-V-acylase and aminoacylase, isolated from the actinomycete Streptoverticillium No 62, revealed the difference in pH and temperature optima, in the sensitivity to the ionic composition of buffer solutions, in the enzyme stability during storage. As for the aminoacylase preparation, its thermostability was studied at different pH values, as well as the effect of specific compounds was tested. Similar to other fungal enzymes, the aminoacylase possesses a wide substrate specificity, and by its stereospecificity can be related to L-aminoacylases, while penicillin-V-acylase is a high-specific enzyme, active against phenoxymethylpenicillin.
D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D002021:Buffers; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D010399:Penicillin Amidase / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D010404:Penicillin V / Q000378:metabolism; D013306:Streptomycetaceae / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
D002021:Buffers; D000581:Amidohydrolases; D010399:Penicillin Amidase; C019672:aminoacylase I; D010404:Penicillin V
Izuchenie svoĭstv preparatov atsilaz aktinomitsetnoĭ kul'tury.