Isolation and purification of α-glucosidase inhibiting components from oyster protein hydrolysate
HU Jian-en, MA Chi-yu, WANG Gang, QU Min, XIE Zhi-fen , WANG Jia-pei , TONG Chang-qing
1. School of Food Engineering, Dalian Fisheries Univ. , Dalian 116023, China;2. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China
Abstract: Water - soluble proteins were produced from soft part of oyster ( Ostrea talienwhanensis crosse) by ammonium sulfate precipitation method. A part of component of the pepsin hydrolyzed oyster protein was found to have a -glucosidase inhibiting activity with IC50 value of 40 mg/mL. However, the MALDI- TOF/MS analysis revealed that there were four mass -to -charge in the ultimate chromatographic absorption peaks on ion -exchange HPLC. The structure of the pepsin hydrolyzed oyster protein was not analyzed because the pepsin hydrolyzed oyster protein was not a single compound. The α - glucosidase inhibiting activity of the oyster protein hydrolysate showed the feasibility of empoldering hypoglycemic product.