Abstract
Lysozyme from Filipino venus (Ruditapes philippinarum) was purified by ion-exchange and gel filtration chromatography. The purification fold and yield were 3,402 and 32.4%, respectively. The molecular weight was determined to be 13.4 kDa by SDS-PAGE. The specific activity of lysozyme was 3.76×105 units/mg protein with Micrococcus lysodeikticus as a substrate. The optimum temperature and pH of lysozyme were 75°C and 5.5, respectively. Lysozyme activity was decreased with about 45% after heat treatment for 30 min at 80°C, and completely inactivated at 100°C. It was activated by NaCl (10–70 mM), MgCl2, and CaCl2 (2–5 mM) whereas it was inhibited by ZnCl2 (2–30 mM).
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.
