牡蛎蛋白水解产物中α-葡萄糖苷酶活性抑制组分的分离与纯化

摘要

Water - soluble proteins were produced from soft part of oyster (Ostrea talienwhanensis crosse) by ammo-nium sulfate precipitation method. A part of component of the pepsin hydrolyzed oyster protein was found to have a α- glucosidase inhibiting activity with IC_(50) 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 feasi-bility of empoldering hypoglycemic product.%采用硫酸铵沉淀法从大连湾牡蛎Ostrea talienwhanensis crosse软体部分中获得水溶性蛋白质,发现胃蛋白酶水解牡蛎蛋白质产物的部分组分具有α-葡萄糖苷酶(AGD)抑制活性,其AGD抑制活性IC_(50)值为40 mg/mL.经过色谱分离纯化,并经MALDI-TOF/MS质谱检测,最终在离子交换HPLC纯化中反映出的单一吸收峰,表现出4个核质比不同的质谱峰,说明是非单一物质,因而没有进行结构分析.根据牡蛎蛋白质水解产物的AGD抑制作用,牡蛎蛋白具有开发为降血糖产品的可能性.