A fermentation medium balanced by the main components was developed for Cryptococcus diffluens strains producing penicillin-V-acylases (PA). It was shown that the culture needed for production of the enzyme was inductor, which was phenoxyacetic acid (POAA). Additional introduction of ethanol to the medium provided an increase in production of PA by 36 per cent and the culture growth by 25 per cent.
View Article and Find Full Text PDFA correlation between the synthesis and secretion of penicillin acylase (PA; EC 3.5.1.
View Article and Find Full Text PDFDynamics of free amino acid utilization by isogenic strains of Escherichia coli differing in intensity of their growth and levels of penicillin acylase biosynthesis in media containing corn steep liquor or peptone was studied. It was shown that in both the media some amino acids such as serine, threonine, glutaminic and asparaginic acids were actively utilized by the strains mainly during the culture intensive growth while others such as glycine, alanine and tyrosine were actively utilized during the enzyme biosynthesis. Intensively utilized arginine and proline were probably used for the growth and biosynthesis.
View Article and Find Full Text PDFFor using actinomyceteous extracellular aminoacylase in production of optically active amino acids it is necessary to have the fermentation broth with lowered contents of extracellular pigments whose accumulation dynamics in the process of the strain growth correlates with the dynamics of the enzyme biosynthesis. The results of the studies showed that it was possible to regulate biosynthesis of the aminoacylase and pigments in the direction of increasing the enzyme production and decreasing the pigment formation by using a medium of the respective composition and providing the respective high temperature and sufficient aeration for the strains.
View Article and Find Full Text PDFPrikl 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.
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