Purification and characterization of penicillin V acylase from Streptomyces lavendulae

Penicillin V acylase was isolated and purified from culture supernatants of Streptomyces lavendulae. The enzyme that is largely extracellular was purified to homogeneity. Two substrates penicillin V and NIPOAB were used for inhibition studies. The kinetic constants were: K-M(penV)=4.9mM, V-max(penV)=0.47 mu mol.min(-1).mg(-1); K-M(NIPOAB)=11.9mM and V-max(NIPOAB)=4.94x10(3) mu mol.min(-1).mg(-1). Penicillin G, phenoxyacetic acid, phenylacetic acid and 6-APA were competitive inhibitors but they inhibited slightly the enzyme. This results were interesting for the possible use of this penicillin V acylase in industrial biorreactors.