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Characterization of the angiotensin-converting enzyme inhibitory activity of fermented milks produced with Lactobacillus casei.

Authors
  • Li, Changkun1
  • Kwok, Lai-Yu1
  • Mi, Zhihui1
  • Bala, Jinnima2
  • Xue, Jiangang2
  • Yang, Jie2
  • Ma, Yuzhu1
  • Zhang, Heping3
  • Chen, Yongfu4
  • 1 Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education P. R. C., Huhhot 010018, P. R. China; Key Laboratory of Dairy Products Processing, Ministry of Agriculture P. R. C., Inner Mongolia Agricultural University, Huhhot 010018, P. R. China. , (China)
  • 2 Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education P. R. C., Huhhot 010018, P. R. China. , (China)
  • 3 Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education P. R. C., Huhhot 010018, P. R. China; Key Laboratory of Dairy Products Processing, Ministry of Agriculture P. R. C., Inner Mongolia Agricultural University, Huhhot 010018, P. R. China. Electronic address: [email protected] , (China)
  • 4 Key Laboratory of Dairy Biotechnology and Engineering, Ministry of Education P. R. C., Huhhot 010018, P. R. China; Key Laboratory of Dairy Products Processing, Ministry of Agriculture P. R. C., Inner Mongolia Agricultural University, Huhhot 010018, P. R. China. Electronic address: [email protected] , (China)
Type
Published Article
Journal
Journal of Dairy Science
Publisher
American Dairy Science Association
Publication Date
Dec 01, 2017
Volume
100
Issue
12
Pages
9495–9507
Identifiers
DOI: 10.3168/jds.2017-12970
PMID: 28964517
Source
Medline
Keywords
License
Unknown

Abstract

Our study assayed angiotensin-converting enzyme (ACE) inhibitory activity and fermentation characteristics of 41 food-originated Lactobacillus casei strains in fermented milk production. Twenty-two of the tested strains produced fermented milks with a high ACE inhibitory activity of over 60%. Two strains (IMAU10408 and IMAU20411) expressing the highest ACE inhibitory activity were selected for further characterization. The heat stability (pasteurization at 63°C for 30 min, 75°C for 25 s, and 85°C for 20 s) and resistance to gastrointestinal proteases (pepsin, trypsinase, and sequential pepsin/trypsinase treatments) of the ACE inhibitory activity in the fermented milks produced with IMAU10408 and IMAU20411 were determined. Interestingly, such activity increased significantly after the heat or protease treatment. Because of the shorter milk coagulation time of L. casei IMAU20411 (vs. IMAU10408), it was selected for optimization experiments for ACE inhibitory activity production. Our results show that fermentation temperature of 37°C, inoculum density of 1 × 106 cfu/g, and fermentation time of 12 h were optimal for maximizing ACE inhibitory activity. Finally, the metabolite profiles of L. casei IMAU20411 after 2 and 42 h of milk fermentation were analyzed by ultra-HPLC electron spray ionization coupled with time-of-flight mass spectrometry. Nine differential abundant metabolites were identified, and 2 of them showed a strong and positive correlation with fermented milk ACE inhibitory activity. To conclude, we have identified a novel ACE inhibitory L. casei strain, which has potential for use as a probiotic in fermented milk production.

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