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基于 MALDI-TOF-MS/MS 从牛乳酪蛋白中鉴定得到的血管紧张素 I 转换酶抑制肽。

Angiotensin I-converting enzyme inhibitory peptides derived from bovine casein and identified by MALDI-TOF-MS/MS.

机构信息

Food Science and Technology Department of Marine Sciences School, Ningbo Universit, Ningbo, China.

出版信息

J Sci Food Agric. 2013 Apr;93(6):1331-7. doi: 10.1002/jsfa.5894. Epub 2012 Sep 26.

DOI:10.1002/jsfa.5894
PMID:23015408
Abstract

BACKGROUND

Hypertension is a major and common threat to the health of individuals around the world. Although agents such as captopril have been shown to regulate high blood pressure effectively, they bring unfavourable side effects such as dry cough and angioedema. If angiotensin I-converting enzyme (ACE) inhibitors derived from natural substances such as milk proteins can be shown to be safe and efficient at managing hypertension, such inhibitors will be a valuable auxiliary to agents such as captopril.

RESULTS

Low-molecular-weight casein-derived peptides hydrolysed by cell envelope proteinase of Lactobacillus casei subsp. casei (ATCC 15008) showed quite high ACE-inhibitory activity. The peptide fraction from α-casein with molecular weight between 5 and 10 kDa showed the highest ACE-inhibitory activity of 82.35%, with a 50% inhibition concentration (IC50 ) of 2.36 mg mL(-1). Peptides from β-casein exhibited lower ACE-inhibitory activity (56.67%, IC50 4.00 mg mL(-1)). Three distinct peptide sequences derived from α-casein (α(s1) -cn f95-105, f106-115 and f148-166) were identified using two-dimensional gel electrophoresis coupled with matrix-assisted laser desorption/ionisation time-of-flight tandem mass spectrometry.

CONCLUSION

This work investigated the ACE-inhibitory properties of casein-derived peptides. Three distinct peptide sequences derived from α-casein were identified. Characterisation of such peptides furthers the investigation of casein-derived ACE-inhibitory peptides from fermented dairy products.

摘要

背景

高血压是全球个体健康的主要且常见威胁。尽管卡托普利等药物已被证明能有效调节高血压,但它们会带来干咳和血管性水肿等不良副作用。如果能证明源自牛奶蛋白等天然物质的血管紧张素 I 转化酶(ACE)抑制剂在治疗高血压方面安全且有效,那么这些抑制剂将成为卡托普利等药物的有益辅助。

结果

经干酪乳杆菌亚种(ATCC 15008)细胞外膜蛋白酶水解的低分子量酪蛋白衍生肽显示出相当高的 ACE 抑制活性。分子量在 5 到 10 kDa 之间的α-酪蛋白肽段表现出最高的 ACE 抑制活性,为 82.35%,半数抑制浓度(IC50)为 2.36mg/mL。β-酪蛋白衍生肽表现出较低的 ACE 抑制活性(56.67%,IC50 为 4.00mg/mL)。使用二维凝胶电泳结合基质辅助激光解吸/电离飞行时间串联质谱鉴定了三种源自α-酪蛋白的不同肽序列(α(s1)-cn f95-105、f106-115 和 f148-166)。

结论

本研究调查了酪蛋白衍生肽的 ACE 抑制特性。鉴定了三种源自α-酪蛋白的不同肽序列。对这些肽的特性描述进一步研究了发酵乳制品中酪蛋白衍生的 ACE 抑制肽。

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