Abstract
An enzyme with improved characteristics is required for biochemical processes to be economically feasible. In this study, improvements in both the stability and activity of Candida antarctica lipase B (CALB) were integrated through multiple-site mutagenesis. CALB was divided into two regions to optimize its performance. Modulating the flexibility within the substrate-binding region and the hydrophilic solvent-affecting region can enhance the catalytic activity and organic solvent stability of CALB, respectively. Combining the mutation sites from the substrate-binding region and from the hydrophilic solvent-affecting region yielded an enzyme (V139E,A92E) with improved functionality. These findings suggest that the characteristics of CALB can be augmented by modulating its flexibility, and this method can possibly be applied to other lipases.
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.
