Optimizing the Hydrolytic Condition of Preparing the ACE Inhibitory Peptides from Casein
Wei Hong, Zhenglian Xue, Ling Chen
Abstract
Wei Hong, Zhenglian Xue, Ling Chen
Abstract
ACE inhibitory peptides were prepared from casein protein by four commercial proteases (alcalase, trypsin, neutrase, alcalase (Novozymes)), and their ACE inhibitory activity were determined in vitro by high-performance liquid chromatography. The result indicated that the ACE inhibitory activity of casein's hydrolysates were 90.4%、83.2%、54.26%、 92.7% by using alcalase、trypsin、neutrase and alcalase (Novozymes) respectively. The optimum hydrolysis conditions of casein of alcalase were studied by the orthogonal design. The result showed that the ACE inhibitory activity of the alcalase's hydrolysates of casein can reach 95.60% under hydrolytic temperature 50℃, E/S 6% and hydrolytic pH10.0 conditions after hydrolyzing 6 hours.
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ACE inhibitory peptides were prepared from casein protein by four commercial proteases (alcalase, trypsin, neutrase, alcalase (Novozymes)), and their ACE inhibitory activity were determined in vitro by high-performance liquid chromatography. The result indicated that the ACE inhibitory activity of casein's hydrolysates were 90.4%、83.2%、54.26%、 92.7% by using alcalase、trypsin、neutrase and alcalase (Novozymes) respectively. The optimum hydrolysis conditions of casein of alcalase were studied by the orthogonal design. The result showed that the ACE inhibitory activity of the alcalase's hydrolysates of casein can reach 95.60% under hydrolytic temperature 50℃, E/S 6% and hydrolytic pH10.0 conditions after hydrolyzing 6 hours.
Key concepts: Chemistry, Casein, Hydrolysis, Hydrolysate, Trypsin, Chromatography, Enzyme, Proteases