Biosynthesis of benzylpenicillin acylase by Escherichia coli NCIM-2400.
Fermentation parameters for the production of penicillin G acylase by Escherichia coli NCIM 2400 have been evaluated. The bacterium produced the enzyme intracellularly when grown in nutrient broth containing PAA. PAA stimulated the enzyme synthesis by 8-10 fold and reduced the lag period. The optimum concentration of PAA for induction was 20 mM and addition of PAA prior to inoculation gave maximum production of PGA. Glucose, lactose, sorbitol, acetate and lactate even at 0.1% concentration catabolically repressed the enzyme formation. Peptone was the best utilised 'N' source for the enzyme production. Phosphate and yeast extract were found to be essential for both the growth and for enzyme biosynthesis. Temperature between 22-24 degrees C was optimum and under ideal condition E. coli NCIM 2400 produced 0.45-0.55 U/ml of penicillin G acylase.
Sudhakaran
V K
VK
Borkar
P S
PS
D000581:Amidohydrolases / Q000096:biosynthesis*; D004926:Escherichia coli / Q000201:enzymology*; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010399:Penicillin Amidase / Q000096:biosynthesis*; D010400:Penicillin G / Q000378:metabolism*; D010648:Phenylacetates / Q000494:pharmacology
D010648:Phenylacetates; D000581:Amidohydrolases; D010399:Penicillin Amidase; C025136:phenylacetic acid; D010400:Penicillin G