Dataset Information

Novel Angiotensin-Converting Enzyme-Inhibitory Peptides From Fermented Bovine Milk Started by Lactobacillus helveticus KLDS.31 and Lactobacillus casei KLDS.105: Purification, Identification, and Interaction Mechanisms.

ABSTRACT: Fermented milks with strong angiotensin I-converting enzyme (ACE)-inhibitory activity were obtained through a culture with Lactobacillus helveticus KLDS.31 and Lactobacillus casei KLDS.105 with a fermentation and storage temperature of 37 °C. Ultrafiltration fractions with a molecular weight less than 3 kDa in fermented milk whey exhibited the strongest inhibitory activity. Correspondingly, a gastrointestinal digestion experiment showed retention of the bioactivity of these fractions with pepsin and trypsin treatment. Four ACE-inhibitory peptides from fermented milk were isolated, purified by two-step reverse chromatography, and sequenced. Furthermore, the interaction mechanisms between ACE and four isolated peptides were investigated by a molecular docking method and the Independent Gradient Model. Experimental determination of IC50 was done to verify theoretical results. The inhibitory peptide interacted with ACE as follows: Lys-Pro-Ala-Gly-Asp-Phe > Lys-Ala-Ala-Leu-Ser-Gly-Met > Lys-Lys-Ala-Ala-Met-Ala-Met > Leu-Asp-His-Val-Pro-Gly-Gly-Ala-Arg.

SUBMITTER: Li J

PROVIDER: S-EPMC6892751 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Novel Angiotensin-Converting Enzyme-Inhibitory Peptides From Fermented Bovine Milk Started by Lactobacillus helveticus KLDS.31 and Lactobacillus casei KLDS.105: Purification, Identification, and Interaction Mechanisms.

Li Jiaqi J Zhao Jiajia J Wang Xindi X Qayum Abdul A Hussain Muhammad Altaf MA Liang Guizhao G Hou Juncai J Jiang Zhanmei Z Li Aili A

Frontiers in microbiology 20191128

Fermented milks with strong angiotensin I-converting enzyme (ACE)-inhibitory activity were obtained through a culture with Lactobacillus helveticus KLDS.31 and Lactobacillus casei KLDS.105 with a fermentation and storage temperature of 37 °C. Ultrafiltration fractions with a molecular weight less than 3 kDa in fermented milk whey exhibited the strongest inhibitory activity. Correspondingly, a gastrointestinal digestion experiment showed retention of the bioactivity of these fractio ...[more]

PMID: 31849852

Similar Datasets

Project description:Koumiss is a traditionally fermented mare's milk described with health-promoting potentials for decades. However, only a few studies focused on the probiotic strains isolated from koumiss. In this study, we collected koumiss samples from Inner Mongolian pasturing area of China and selected a promising strain of Lactobacillus helveticus, isolate NS8, based on the survival abilities in gastrointestinal tract (GIT) and adhesion to intestinal endothelial cells in vitro. As the ability to positively modulate host immune response is a feature of increasing importance in measuring the probiotic potential of a bacterial strain, our study mainly focus on the immunomodulatory properties of L. helveticus NS8 by using in vivo and ex vivo analyses.L. helveticus NS8 was identified by molecular-typing methods, both at genus and species levels. As a typical food niche-specific bacteria, NS8 showed a moderate survival ability in GIT environment in vitro. However, an excellent binding capacity to the human intestinal epithelial cells, along with significant autoaggregation and cell-surface hydrophobicity was observed. Additionally, the presence of S-layer protein was responsible for the cell surface properties of this strain. NS8 was found to be rather protective against TNBS (2,4,6-trinitrobenzene sulfonic acid)-induced murine colitis. In the meantime, co-culture with NS8 induced an increased level of secretion of anti-inflammatory cytokine IL-10 in peripheral blood mono-nuclear cells (PBMCs). Furthermore, NS8 was also able to diminish the proinflammatory effects of lipopolysaccharide (LPS) in mouse macrophage cell line RAW264.7 by inducing higher levels of IL-10. Specially, adding of the purified S-layer protein didn't influence the production of IL-10. The specific ligand-host receptor interactions on the NS8 specific immune responses need to be learned further.In summary, L. helveticus NS8 exhibited good probiotic and particularly immunomodulatory properties, with a potential for development of functional food commercially or therapeutic adjuvant for inflammatory diseases.

Project description:Peptides in the 3-kDa ultrafiltrate of fermented whey protein isolate (WPI) medium could be responsible for the antivirulence activity of Lactobacillus helveticus LH-2 and Lactobacillus acidophilus La-5 against Salmonella Typhimurium. Non-fermented and fermented media containing 5.6% WPI were fractionated at a 3 kDa cut-off and the filtrate was analyzed by mass spectrometry. The non-fermented WPI medium contained 109 milk derived peptides, which originated from ?-casein (52), ?s1-casein (22), ?s2-casein (10), ?-casein (8), and ?-lactoglobulin (17). Most of these peptides were not found in the fermented media, except for 14 peptides from ?-casein and one peptide from ?s2-casein. Database searches confirmed that 39 out of the 109 peptides had established physiological functions, including angiotensin-converting-enzyme (ACE) inhibitory, antioxidant, antimicrobial, or immunomodulating activity. A total of 75 peptides were found in the LH-2 cell free spent medium (CFSM): 54 from ?-casein, 14 from k-casein, 4 from ?-lactoglobulin and 3 from ?s2-casein. From these peptides, 19 have previously been associated with several categories of bioactivity. For La-5 CFSM, a total of 15 peptides were sequenced: 8 from ?-casein, 5 from ?s1-casein, 2 from ?-lactoglobulin. Only 5 of these have previously been reported as having bioactivity. Many of the peptides remaining in the fermented medium would contain low-affinity residues for oligopeptide binding proteins and higher resistance to peptidase hydrolysis. These properties of the sequenced peptides could explain their accumulation after fermentation despite the active proteolytic enzymes of LH-2 and La-5 strains. Down-regulated expression of hilA and ssrB genes in S. Typhimurium was observed in the presence of La-5 and LH-2 CFSM. Downregulation was not observed for the Salmonella oppA mutant strain exposed to the same CFSM used to treat the S. Typhimurium DT104 wild-type strain. This result suggests the importance of peptide transport by S. Typhimurium for down regulation of virulence genes in Salmonella.

Dataset Information

Novel Angiotensin-Converting Enzyme-Inhibitory Peptides From Fermented Bovine Milk Started by Lactobacillus helveticus KLDS.31 and Lactobacillus casei KLDS.105: Purification, Identification, and Interaction Mechanisms.

Publications

Novel Angiotensin-Converting Enzyme-Inhibitory Peptides From Fermented Bovine Milk Started by <i>Lactobacillus helveticus</i> KLDS.31 and <i>Lactobacillus casei</i> KLDS.105: Purification, Identification, and Interaction Mechanisms.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets