Abstract
Penicillin Vacylase isolated from Streptomyces lavendulae is an extracellular enzyme with interesting properties for the industrial production of 6-APA. The enzyme hydrolysed penicillin V and synthetic analogues such as 2-nitro-5-(phenoxyacetarnido)-benzoic acid (NTPOAB). The corresponding kinetic parameters were KM = 3 mM and V max = 92 μmol min-1 mg-1 for penicillin V; KM = 15.3 mM and V max = 14.5 μmol. min-1 mg-1 for NIPOAB. Studies of inhibition by products, alternative products and dead-end inhibition supported an ordered uni bi mechanism that could involve an acyl-enzyme intermediate as has been described for penicillin G acylases and other amidases.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
