ArticleKorean journal for food science of animal resources2015
Identification of Antihypertensive Peptides Derived from Low Molecular Weight Casein Hydrolysates Generated during Fermentation by Bifidobacterium longum KACC 91563.
Article in Korean journal for food science of animal resources, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Peptidome and Metabolome Profiling of Fermented Milk Products Reveal Accumulation of Bioactive Compounds During Cold Storage.Current issues in molecular biology · 2026Article
- Koumiss (Fermented Mare's Milk) as a Functional Food: Bioactive Proteins, Peptides, and Future Perspectives.Foods (Basel, Switzerland) · 2025Review
- Food-Derived Opioid Peptides in Human Health: A Review.International journal of molecular sciences · 2020Review
- Transport of a Peptide from Bovine αNutrients · 2020Article
- Enhanced Production of Galactooligosaccharides Enriched Skim Milk and Applied to Potentially Synbiotic Fermented Milk withFood science of animal resources · 2019Article
- Use of Mass Spectrometry to Profile Peptides in Whey Protein Isolate Medium Fermented byFrontiers in nutrition · 2019Article
- Antihypertensive peptides from whey proteins fermented by lactic acid bacteria.Food science and biotechnology · 2018Article
- Article
- κ-Casein as a source of short-chain bioactive peptides generated byJournal of food science and technology · 2017Article
- Identification and Characterization of a Novel Antioxidant Peptide from Bovine Skim Milk Fermented byKorean journal for food science of animal resources · 2017Article
- Characteristics of Kwark Cheese Supplemented withKorean journal for food science of animal resources · 2017Article
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7 authors.
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Abstract
Angiotensin-converting enzyme (ACE) inhibitory activity was evaluated for the low-molecular-weight fraction (<3 kDa) obtained from milk fermentation by Bifidobacterium longum KACC91563. The ACE inhibitory activity in this fraction was 62.3%. The peptides generated from the <3 kDa fraction were identified by liquid chromatography-electrospray ionization quantitative time-of-flight mass spectrometry analysis. Of the 28 peptides identified, 11 and 16 were identified as β-casein (CN) and αs1-CN, respectively. One peptide was identified as κ-CN. Three peptides, YQEPVLGPVRGPFPIIV, QEPVLGPVRGPFPIIV, and GPVRGPFPIIV, from β-CN corresponded to known antihypertensive peptides. We also found 15 peptides that were identified as potential antihypertensive peptides because they included a known antihypertensive peptide fragment. These peptides were as follows: RELEELNVPGEIVE (f1-14), YQEPVLGPVRGPFP (f193-206), EPVLGPVRGPFPIIV (f195-206), PVLGPVRGPFPIIV (f196-206), VLGPVRGPFPIIV (f197-206), and LGPVRGPFPIIV (f198-206) for β-CN; and APSFSDIPNPIGSENSEKTTMPLW (f176-199), SFSDIPNPIGSENSEKT- TMPLW (f178-199), FSDIPNPIGSENSEKTTMPLW (f179-199), SDIPNPIGSENSEKTTMPLW (f180-199), DIPNPIGSENSEKTTMPLW (f181-199), IPNPIGSENSEKTTMPLW (f182-199), PIGSENSEKTTMPLW (f185-199), IGSENSEKTTMPLW (f186-199), and SENSEKTTMPLW (f188-199) for αs1-CN. From these results, B. longum could be used as a starter culture in combination with other lactic acid bacteria in the dairy industry, and/or these peptides could be used in functional food manufacturing as additives for the development of a product with beneficial effects for human health.
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