Abstract
The immobilization of enzyme with enhanced catalytic activity is the major challenge. In this work, we have activated the lipase in the presence of proline and successfully immobilized into zeolitic imidazolate framework (ZIF)-8 by biomineralization method. The prepared lipase–proline MOF exhibited 135% enhanced catalytic activity as compared to free counterpart. Further, it exhibited four-fold improved thermal stability with respect to native enzyme after immobilization. In Michaelis–Menten kinetic studies, Km values for lipase–proline MOF were found to be lower, whereas, it exhibited higher Vmax than lipase–MOF and free lipase. The lipase–MOF and lipase–proline MOF were showed 56% and 72% residual activity, respectively after six cycles of reuse.
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 callMore From: International Journal of Biological Macromolecules
Disclaimer: 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.
