Angiotensin-converting enzyme inhibitory peptides from Lactobacillus delbrueckii QS306 fermented milk

Angiotensin-converting enzyme inhibitory peptides were isolated and identified from milk fermented using Lactobacillus delbrueckii QS306. The peptide with the highest angiotensin-converting enzyme inhibitory activity (C5) was purified using ultrafiltration with 10 and 3 kDa molecular mass cut-off me...

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Bibliographic Details
Published in:Journal of dairy science 2019-07, Vol.102 (7), p.5913-5921
Main Authors: Wu, Nan, Xu, Weihan, Liu, Kangling, Xia, Yanan, Shuangquan
Format: Article
Language:English
Subjects:
angiotensin-converting enzyme inhibitory peptide
fermented milk
identification
Lactobacillus delbrueckii QS306
purification
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Summary:Angiotensin-converting enzyme inhibitory peptides were isolated and identified from milk fermented using Lactobacillus delbrueckii QS306. The peptide with the highest angiotensin-converting enzyme inhibitory activity (C5) was purified using ultrafiltration with 10 and 3 kDa molecular mass cut-off membranes, Sephadex G-15 (Sigma-Aldrich, St. Louis, MO) gel filtration chromatography, reversed-phase HPLC, and Orbitrap Elite (Thermo Fisher Scientific Inc., Waltham, MA) liquid chromatography-tandem mass spectrometry. We obtained peptide LPYPY by microbial fermentation, which was derived from κ-casein f (AA 77–81). We synthesized LPYPY using an Fmoc solid-phase synthesis method and explored the secondary structure of the pentapeptide. The half maximal inhibitory concentration for the angiotensin-converting enzyme inhibitory activity of LPYPY was 12.87 μg/mL. The results provide additional information for ongoing research and the development of functional foods having antihypertensive effects.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.2018-15901