4.7 Article

Development of Antioxidant and Antihypertensive Properties during Growth of Lactobacillus helveticus, Lactobacillus rhamnosus and Lactobacillus reuteri on Cow's Milk: Fermentation and Peptidomics Study

Journal

FOODS
Volume 10, Issue 1, Pages -

Publisher

MDPI
DOI: 10.3390/foods10010017

Keywords

Lactobacillus; milk fermentation; proteolytic activity; antioxidant activity; angiotensin-converting enzyme inhibitory activity (ACE-I); peptidomics; bioactive peptides

Funding

  1. Russian Science Foundation [16-16-00094]
  2. Russian Science Foundation [16-16-00094] Funding Source: Russian Science Foundation

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Bioactive peptides derived from milk proteins have positive effects on various physiological systems and are considered promising ingredients for functional food. These peptides are usually inactive within parent proteins and can be released during milk fermentation by specific proteolytic systems of different Lactobacillus spp.
Bioactive peptides derived from milk proteins are an active research area. Exhibiting numerous positive physiological effects on digestive, cardiovascular, immune and nervous systems, these peptides thought to be one of the most promising ingredients for functional food. Generally, these peptides are inactive within the parent proteins and can be liberated during milk fermentation by the specific proteolytic systems of various Lactobacillus spp. Here we present the study of milk fermentation by Lactobacillus helveticus NK1, Lactobacillus rhamnosus F and Lactobacillus reuteri LR1 strains. It was demonstrated that the antioxidant activity of the milk fermented by these strains concomitantly increased with the strains' proteolytic activity. For the angiotensin I-converting enzyme (ACE) inhibitory activity, the same tendency was not observed. Although the proteolytic activity of L. helveticus NK1 was two times higher than that of L. rhamnosus F, the milk fermented by these strains showed comparable ACE inhibition. The analysis of the peptide profiles of the fermented milk samples allowed us to hypothesize that some previously unreported peptides can be produced by L. rhamnosus F. In addition, it was demonstrated that these potential ACE-inhibiting peptides originated from the C-terminus of alpha(S2)-casein.

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