Prikl Biokhim Mikrobiol
March 1985
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.
View Article and Find Full Text PDFA procedure for highly purified cephalexin amidase of Xanthomonas was developed. It consists of preparation of a cell-free extract of the culture after cell disintegration, precipitation with ammonium sulfate, dissolution, concentration and elimination of ballast proteins, gel filtration on Sephadex G-25, sorption of ballast proteins on DEAE cellulose and chromatography on KM-cellulose. The enzyme yield is 45-55 per cent.
View Article and Find Full Text PDFThe procedure for isolation of acylases from the fermentation broth filtrates of 3 actinomycetous cultures was developed with a yield of 72-97 per cent and 11-19- fold purification of the preparations. Comparative study of substrate specificity of acylase preparations showed that all of them possessed 2 types of the activity, i.e.
View Article and Find Full Text PDFThe acylase activity of 113 actinomycetous strains and 71 bacterial strains was studied. A number of strains producing acylases, hydrolyzing phenoxymethylpenicillin was detected among the actinomycetous cultures and a number of strains producing acylases active against ampicillin and benzylpenicillin was detected among the bacterial cultures. These acylases may be used in production of semisynthetic beta-lactam antibiotics and their semiproducts.
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