Abstract
The role of exposed tyrosine side-chains in enzyme-catalyzed reaction by sweet almond emulsion β- d-glucosidase (β- d-glucoside glucohydrolase, EC 3.2.1.21) has been studied using N-acetylimidazole as the specific reagent. The changes in activity, binding affinity and kinetic parameters ( K m, V) as a result of acetylation of the phenolic hydroxyl groups have been determined. The acetylation increased the K m values of both β-glucosidase and β-galactosidase activities, whereas V remained unchanged. Similarly, the binding affinity for immobilized phenyl β- d-glucopyranoside decreased appreciably. After the removal of the acetyl groups the enzyme regained 96% of the original activity. It is concluded that the tyrosine moieties, located in the active centre of the enzyme, have both glucoside and galactoside binding functions.
Published Version
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.
