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牛乳酪蛋白源ACE抑制肽的稳定性和毒理特性研究
作者姓名:Wei WU  Pan-pan YU  Feng-yang ZHANG  Hong-xia CHE  Zhan-mei JIANG
作者单位:Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, China
基金项目:Project supported by the Innovative Research Team of Higher Edu- cation of Heilongiiang Province (No. 2010tdl 1 ), the National Natural Science Foundation of China (No. 31000801), the National Key Technology R&D Program of China during the 12th Five-Year Plan Period (No. 2013BAD18B06), and the 2009 Doctoral Science Re- search of Northeast Agricultural University, China
摘    要:研究目的:创新要点:研究方法:重要结论:酸碱热处理对牛乳酪蛋白源血管紧张素转化酶(ACE)抑制肽的抑制活性、游离氨基、色泽及其毒理特性的影响。在pn9.0-12.0的热处理条件下,牛乳酪蛋白源ACE抑制肽的抑制活性降低,色泽加深。热处理后的ACE抑制肽对Caco-2细胞和ECV-304细胞没有毒性作用。以ACE抑制活性、游离氨基、色差值和细胞存活率为检测指标,研究了酸碱热处理对ACE抑制肽的稳定性和毒理特性影响。高温和碱性热处理能破坏酪蛋白源ACE抑制肽的稳定性(见图1~3)。

关 键 词:血管紧张素转化酶(ACE)抑制肽  热处理  稳定性  毒理特性

Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein
Wei WU,Pan-pan YU,Feng-yang ZHANG,Hong-xia CHE,Zhan-mei JIANG.Stability and cytotoxicity of angiotensin-I-converting enzyme inhibitory peptides derived from bovine casein[J].Journal of Zhejiang University Science,2014(2):143-152.
Abstract: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.
Keywords:Angiotensin-l-converting enzyme inhibitory peptide  Heat treatment  Stability  Cytotoxicity
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