Abstract
Enzyme inactivation has been observed in the course of penicillin acylase-catalyzed hydrolysis and aminolysis of d-phenylglycine amide. Inactivation was very sensitive to the d-phenylglycine amide concentration: at pH 9.5, 25 °C and 400 mM substrate, penicillin acylase lost more than 90% of its initial catalytic activity in half an hour, in the presence of 100 mM substrate, 50% of the initial activity in two hours, whereas in the absence of substrate, no significant enzyme inactivation was observed in three hours. Observed enzyme inactivation limits use of high acyl donor concentrations at penicillin acylase-catalyzed peptide synthesis.
Sign-in/Register to access full text options 
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.
