This study investigated the effect of heat treatment combined with acid and alkali on the angiotensin-I- converting enzyme （ACE） inhibitory activity of peptides derived from bovine casein. The free amino group conte...This study investigated the effect of heat treatment combined with acid and alkali on the angiotensin-I- converting enzyme （ACE） inhibitory activity of peptides derived from bovine casein. The free amino group content, color, and cytotoxicity of the peptides were measured under different conditions. When heated at 100 ℃ in the pH range from 9.0 to 12.0, ACE inhibitory activity was reduced and the appearance of the peptides was significantly darkened. After thermal treatment in the presence of acid and alkali, the free amino group content of ACE inhibitory peptides decreased markedly. High temperature and prolonged heating also resulted in the loss of ACE inhibitory activity, the loss of free amino groups, and the darker coloration of bovine casein-derived peptides. However, ACE inhibitory peptides, within a concentration range of from 0.01 to 0.2 mg/ml, showed no cytotoxicity to Caco-2 and ECV-304 cell lines after heat treatment. This indicated that high temperature and alkaline heat treatment impaired the stability of bovine casein-derived ACE inhibitory peptides.展开更多
基金supported by the Innovative Research Team of Higher Education of Heilongjiang Province(No.2010td11)the National Natural Science Foundation of China(No.31000801)+1 种基金the National Key Technology R&D Program of China during the 12th Five-Year Plan Period(No.2013BAD18B06)the 2009 Doctoral Science Research of Northeast Agricultural University,China
文摘This study investigated the effect of heat treatment combined with acid and alkali on the angiotensin-I- converting enzyme （ACE） inhibitory activity of peptides derived from bovine casein. The free amino group content, color, and cytotoxicity of the peptides were measured under different conditions. When heated at 100 ℃ in the pH range from 9.0 to 12.0, ACE inhibitory activity was reduced and the appearance of the peptides was significantly darkened. After thermal treatment in the presence of acid and alkali, the free amino group content of ACE inhibitory peptides decreased markedly. High temperature and prolonged heating also resulted in the loss of ACE inhibitory activity, the loss of free amino groups, and the darker coloration of bovine casein-derived peptides. However, ACE inhibitory peptides, within a concentration range of from 0.01 to 0.2 mg/ml, showed no cytotoxicity to Caco-2 and ECV-304 cell lines after heat treatment. This indicated that high temperature and alkaline heat treatment impaired the stability of bovine casein-derived ACE inhibitory peptides.
