Preparation of trehalase inhibitor validoxylamine A by biocatalyzed hydrolysis of validamycin A with honeybee (Apis cerana Fabr.) beta-glucosidase.
Validoxylamine A is structurally similar to trehalose and acts a potent competitive 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, beta-glucosidase extracted from honeybees (Apis cerana Fabr.) was used as a catalyst to produce validoxylamine A through enzymatic hydrolysis of validamycin A. Beta-glucosidase was separated and purified from honeybees, and its characteristics were examined. The results showed that beta-glucosidase was stable across a range of temperatures from 30 to 40 degrees 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 beta-glucosidase revealed that both the substrate (validamycin A) and the product (validoxylamine A) inhibited beta-glucosidase activity. The inhibition constant of the substrate Kis value was 5.01 mM, and that of the product Kip value was 1.32 mM. This product inhibition was competitive.
Xue
Ya-Ping
YP
Institute of Bioengineering, Zhejiang University of Technology, Hangzhou 310014, People's Republic of China.
Zheng
Yu-Guo
YG
Shen
Yin-Chu
YC
D000818:Animals; D001516:Bees / Q000201:enzymology*; D002384:Catalysis; D004791:Enzyme Inhibitors / Q000737:chemistry*; D006868:Hydrolysis; D007294:Inositol / Q000031:analogs & derivatives* / Q000737:chemistry; D019476:Insect Proteins / Q000737:chemistry* / Q000302:isolation & purification; D014198:Trehalase / Q000037:antagonists & inhibitors* / Q000737:chemistry; D001617:beta-Glucosidase / Q000737:chemistry* / Q000302:isolation & purification
D004791:Enzyme Inhibitors; D019476:Insect Proteins; C030790:validamycin A; C052534:validoxylamine A; D007294:Inositol; D001617:beta-Glucosidase; D014198:Trehalase