Abstract
A novel carboxylesterase (EC 3.1.1.1) from Aspergillus niger has been purified 1400-fold by ammonium sulphate fractionation, ion exchange chromatography, hydrophobic interaction chromatography and gel filtration. The enzyme consisted of two identical subunits, each with a molecular weight of 60,000. The isoelectric point was 4.5. The optimal pH for the hydrolysis of cinnamic acid ethyl ester and 2-furylacryloyl N-hydroxy succinimide ester was between 5 and 7. The enzyme, which had no lipase activity, catalyzed the hydrolysis of activated ester substrates where the alcohol moiety was N-hydroxysuccinimide, p-nitrophenol and phenol as well as, with lower rates, unactivated esters like ethyl and benzyl esters. The enzyme exhibited a preference for substrates with an acyl moiety containing an aryl group. The enzyme was inhibited by PMSF but not by Hg2+ and EDTA. It is classified as a serine carboxylesterase.
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.
