𝔖 Bobbio Scriptorium
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Identification of a penicillin V acylase processing fungus

✍ Scribed by E. Stoppok; F. Wagner; F. Zadrazil

Book ID
104789024
Publisher
Springer
Year
1981
Tongue
English
Weight
140 KB
Volume
13
Category
Article
ISSN
1432-0614

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## Penicillin V acylase from jFusarium sp. SKF 235 was i~obilized on several cation-exchange resins, of which Amberlite CG-50 was preferred. Maximum activity of the immobilized penicillin V acylase was 250 to 280 W/g dry beads. The pH and temperature optima of the enzyme shifted from 6.5 to 6.8 a

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Penicillin V acylase was produced, both intracellularly and extracellularly, by Fusarium sp. SKF 235 grown in submerged fermentation. When neopeptone was added to the medium, >95% of the penicillin V acylase was extracellular. In the absence of a complex organic nitrogen source, the fungus produced