摘要
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IC50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。
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.
出处
《大连水产学院学报》
CSCD
北大核心
2009年第5期449-452,共4页
Journal of Dalian Fisheries University
