[Penicillin amidase from E. coli. A direct spectrophotometric method of determining the enzyme's activity].
A method for determination of the enzymatic activity of penicillinamidas (PA) based on spectrophotometric estimation of the stained product amount produced in hydrolysis of 4-phenylacetamido-2-nitrobenzoic acid (PANBA) catalyzed by the enzyme is proposed. Some physico-chemical properties of the substrate and the stained product were studied. The kinetic parameters of the PANABA enzymatic hydrolysis were determined. Catalytic activity of some enzyme products of PA of different purity levels was studied comparatively in reactions of PANBA and benzylpenicillin hydrolysis.
D000581:Amidohydrolases / Q000032:analysis*; D062365:Aminobenzoates; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007202:Indicators and Reagents; D007700:Kinetics; D010399:Penicillin Amidase / Q000032:analysis*; D013053:Spectrophotometry / Q000379:methods*; D013997:Time Factors
D062365:Aminobenzoates; D007202:Indicators and Reagents; D000581:Amidohydrolases; D010399:Penicillin Amidase
Penitsillinamidaza iz E. coli. Priamoĭ spektrofotometricheskiĭ metod opredeleniia aktivnosti fermenta