Abstract: Casein hydrolysates that have the degree of hydrolysis of 13.5 % and IC50 value of 45.23μg/mL were prepared from casein with a protease Alcalase,and then modified by plastein reaction with another protease Neutrase.The effects of the addition level of Neutrase,the concentration of casein hydrolysates,temperature and time on the plastein reaction of casein hydrolysates were studied.The results indicated that hydrolysis reaction was the dominant one in the Plastein reaction system as the content of free amino groups in reaction system increased in all conditions.The addition level of Neutrase,the concentration of casein hydrolysates and reaction time all had significant impact on the plastein reaction of casein hydrolysates,while reaction temperature gave some influence.Under lower addition level of Neutrase,higher concentration of casein hydrolysates and shorter reaction time,the extent of increase in free amino groups in Plastein reaction system tended to decrease which implied that hydrolysis reaction were weakened relatively.Six modified casein hydrolysates with different reaction extents were prepared and their ACE inhibitory activities were determined.The results showed that the values of IC50 of the modified products were in range of 15.56 to 19.98 μg/mL,indicating that the ACE inhibitory activity of casein hydrolysates could be improved significantly by plastein reaction catalyzed by Neutrase.
徐微,赵新淮. 酪蛋白水解物的中性蛋白酶修饰及其ACE抑制活性[J]. 食品与发酵工业, 2010, 36(05): 17-22.
Xu Wei,Zhao Xin-huai. Modification of Casein Hydrolysates by Neutrase and ACE Inhibitory Activity of the Products[J]. Food and Fermentation Industries, 2010, 36(05): 17-22.