Variability of Hydrolysis of 尾-, 伪s1-, and 伪s2-Caseins by 10 Strains of Streptococcus thermophilus and Resulting Bioactive Peptides
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- 作者：Laurent Miclo ; 脡meline Roux ; Magali Genay ; 脡milie Brusseaux ; Chantal Poirson ; Nawara Jameh ; Clarisse Perrin ; Annie Dary
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2012
- 出版时间：January 18, 2012
- 年：2012
- 卷：60
- 期：2
- 页码：554-565
- 全文大小：1093K
- 年卷期：v.60,no.2(January 18, 2012)
- ISSN：1520-5118
文摘
Milk proteins contain numerous potential bioactive peptides, which may be released by digestive proteases or by the proteolytic system of lactic acid bacteria during food processing. The capacity of Streptococcus thermophilus to generate peptides, especially bioactive peptides, from bovine caseins was investigated. Strains expressing various levels of the cell envelope proteinase, PrtS, were incubated with 伪s1-, 伪s2-, or 尾-casein. Analysis of the supernatants by LC-ESI-MS/MS showed that the 尾-casein was preferentially hydrolyzed, followed by 伪s2-casein and then 伪s1-casein. Numbers and types of peptides released were strain-dependent. Hydrolysis appeared to be linked with the accessibility of different casein regions by protease. Analysis of bonds hydrolyzed in the region 1鈥?3 of 伪s1-casein suggests that PrtS is at least in part responsible for the peptide production. Finally, among the generated peptides, 13 peptides from 尾-casein, 5 from 伪s2-casein, and 2 from 伪s1-casein have been reported as bioactive, 15 of them being angiotensin-converting enzyme inhibitors.