首页 | 官方网站   微博 | 高级检索  
     

酪蛋白磷酸肽副产物中ACEI肽的分离鉴定及稳定性研究
引用本文:赵力超,宁德山,龙梓祺,刘飞,陈飞龙,曹庸.酪蛋白磷酸肽副产物中ACEI肽的分离鉴定及稳定性研究[J].现代食品科技,2014,30(10):52-57.
作者姓名:赵力超  宁德山  龙梓祺  刘飞  陈飞龙  曹庸
作者单位:华南农业大学食品学院,广东广州 510642;无限极(中国)有限公司,广东广州 510623;华南农业大学食品学院,广东广州 510642;广州绿萃生物科技有限公司,广东广州 510663;华南农业大学食品学院,广东广州 510642;华南农业大学食品学院,广东广州 510642
基金项目:广东省科技计划项目(2012B020312004)
摘    要:酪蛋白磷酸肽副产物中仍含有丰富的功能性多肽,从中回收具有降压活性的血管紧张素I转化酶抑制肽具有废物利用和环境保护的意义。本文在前期研究富集活性肽工艺的基础上,从粗富集产物中进一步分离纯化出具有降压活性的多肽单体,并对单体的分子量、一级序列及其稳定性进行了研究。研究结果表明,以粗富集产物为原料,仅通过阴离子交换树脂及液相制备两步就可获得活性较高的转化酶抑制肽单体P16和P18。P16分子量742.6,序列为GPFPIIV,属首次发现;P18分子量1385.8,序列为FFVAPFPE VFGK。二者均具有较高的耐酸碱性和热稳定性,经体外模拟胃肠消化过程后,发生不同程度的分解,但P16的活性在分解后反而升高12.8%,P18则降低37.5%。推测活性的升高或降低均与活性中心暴露或破坏有关。

关 键 词:酪蛋白磷酸肽副产物  血管紧张素I转化酶抑制肽  废物利用  降血压  结构分析  稳定性
收稿时间:5/5/2014 12:00:00 AM

Purification, Identification and Evaluation of the Stability of Angiotensin I-converting Enzyme Inhibitory Peptides Derived from By-products of Casein Phosphopeptides
ZHAO Li-chao,NING De-shan,LONG Zi-qi,LIU Fei,CHEN Fei-long and CAO Yong.Purification, Identification and Evaluation of the Stability of Angiotensin I-converting Enzyme Inhibitory Peptides Derived from By-products of Casein Phosphopeptides[J].Modern Food Science & Technology,2014,30(10):52-57.
Authors:ZHAO Li-chao  NING De-shan  LONG Zi-qi  LIU Fei  CHEN Fei-long and CAO Yong
Affiliation:College of Food Science, South China Agricultural University, Guangzhou, Guangdong 510642, China;Infinitus Co., Ltd, Guangzhou, Guangdong 510623, China;College of Food Science, South China Agricultural University, Guangzhou, Guangdong 510642, China;Greencream Biotech Co., Ltd, Guangzhou, Guangdong 510663, China;College of Food Science, South China Agricultural University, Guangzhou, Guangdong 510642, China;College of Food Science, South China Agricultural University, Guangzhou, Guangdong 510642, China
Abstract:By-products of casein phosphopeptide contain abundant functional peptides, from which angiotensin I-converting enzyme (ACE-I) inhibitory peptides with antihypertensive activity can be recycled. This is of significance for utilizing waste and protecting the environment. Based on previous research on technology that accumulates bioactive peptides, the peptide monomers with antihypertensive activity were isolated and purified from crude-enriched products, and the molecular weights of peptide monomers, their primary sequences, and stabilities were studied. The results showed that, using the crude products as raw materials, ACE-I inhibitory peptide monomers with high activity, P16 and P18, could be obtained in just two steps, including anion-exchange chromatography and HPLC. The molecular weight of P16 was 742.6 and its primary sequence was GPFPIIV, which was discovered for the first time. The molecular weight of P18 was 1385.8 and its primary sequence was FFVAPFPEVFGK. Both P16 and P18 possessed high acid-base resistance and thermal stability. Various degrees of decomposition occurred in both peptides in the in vitro gastrointestinal digestion test. Nevertheless, the activity of P16 increased by 12.8%, while that of P18 decreased by 37.5%. Thus, the rise and decline were related to the exposure or destruction of the active centers.
Keywords:casein phosphopeptides by-products  angiotensin-I converting enzyme inhibitory peptides  waste utilization  antihypertension  structure analysis  stability
本文献已被 CNKI 等数据库收录!
点击此处可从《现代食品科技》浏览原始摘要信息
点击此处可从《现代食品科技》下载全文
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司    京ICP备09084417号-23

京公网安备 11010802026262号