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- Publisher
- Springer Journals
- Copyright
- Copyright © 2005 by Humana Press Inc
- Subject
- Chemistry; Biotechnology; Biochemistry, general
- ISSN
- 0273-2289
- eISSN
- 1559-0291
- DOI
- 10.1385/ABAB:127:3:157
- Publisher site
- See Article on Publisher Site
Abstract
Validoxylamine A is structurally similar to trehalose and acts a potent competivive inhibitor of trehalase. It has recently been receiving increased attention as a potential material for the development of new insecticides or drugs. In this study, β-glucosidase extracted from honeybees (Apis cerana Fabr.) was used as a catalyst to produce validoxylamine A through enzymatic hydrolysis of validamycin A. β-Glucosidase was separated and purified from honeybees, and its characteristics were examined. The results showed that β-glucosidase was stable across a range of temperatures from 30 to 40°C and across a relatively wide range of pH values from 5.0 to 7.5. Investigation of the biocatalyzed hydrolysis process from validamycin A to validoxylamine A with β-glucosidase revealed that both the substrate (validamycin A) and the product (validoxylamine A) inhibited β-glucosidase activity. The inhibition constant of the substrate K value was 5.01 mM, and that of the product K ip value was 1.32 mM. This product inhibition was competitive.
Journal
Applied Biochemistry and Biotechnology – Springer Journals
Published: Apr 17, 2007