关键词: 光谱法, DNJ, α-葡萄糖苷酶，降血糖机理

Abstract: we are applying the method of spectrumultraviolet fluorescence, CD to further explore the interaction of DNJ and alpha glycosidase enzymes, the concentration of the partial inhibition of DNJ and α-glucosidase reactions was 0.297 μg/mL. The linewey-burk double-inverse method come to a conclusion that inhibition type of DNJ to α-glucosidase is competitive inhibition. The reaction is static quenching with generating ground-state complexes, which make alpha glycosidase endogenous fluorescence quenched. The process is an entropy-driven endothermic reaction. The main driving factor of the reaction is hydrophobic force. In different temperature (273K,298K,310K), fluorescence quenching kinetic constant Ka is 1.48×104 L·mol-1, 1.29×104 L·mol-1, and 1.12×104 L·mol-1. DNJ make conformation of alpha glycosidase changed, whose secondary structure rearranged. The changed conformation induces the enzyme active pocket to close, and substrate is not good for binding to the active site, this is the mechanization that DNJ lower the activity of alpha glycosidase.

Key words: Spectroscopy, 1-Deoxynojirimycin, α-Glucosidase