Abstract
We report studies of the enzymatic activity of α-chymotrypsin (CHT) in aqueous buffer and AOT reverse micelle with various degrees of hydration using the substrate Ala–Ala–Phe–7-amido-4-methylcoumarin (AMC). From Michaelis–Menten kinetics, we determined equilibrium and rate constants for catalytic activity in aqueous buffer. In the reverse micelle we found that the activity of CHT to be retarded by two orders of magnitude compared to that in aqueous buffer. The activity is also found to be nearly insensitive to the degree of hydration of reverse micelle. From these studies, we attempt to elucidate the influence of hydration on enzyme activity.
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.
