Development of a Soy Protein Hydrolysate with an Antihypertensive Effect

Daliri, Eric Banan‐Mwine; Ofosu, Fred Kwame; Chelliah, Ramachandran; Park, Mi Houn; Kim, Jong-Hak; Oh, Deog‐Hwan

doi:10.3390/ijms20061496

Cited by 54 publications

(22 citation statements)

References 34 publications

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“…Soy protein hydrolysates with antihypertensive properties have also been developed via fermentation of soy protein hydrolysates by Lb. rhamnosus EBD1 (Daliri et al., 2019). Moreover, Setti, Kachouri, and Hamdi (2018) recently reported on the generation of antioxidant peptides through the fermentation of fenugreek proteins with Lc.…”

Section: Applications Of Ceps In Food Technology and Human Healthmentioning

confidence: 99%

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

et al. 2020

Comp Rev Food Sci Food Safe

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Proteins displayed on the cell surface of lactic acid bacteria (LAB) perform diverse and important biochemical roles. Among these, the cell‐envelope proteinases (CEPs) are one of the most widely studied and most exploited for biotechnological applications. CEPs are important players in the proteolytic system of LAB, because they are required by LAB to degrade proteins in the growth media into peptides and/or amino acids required for the nitrogen nutrition of LAB. The most important area of application of CEPs is therefore in protein hydrolysis, especially in dairy products. Also, the physical location of CEPs (i.e., being cell‐envelope anchored) allows for relatively easy downstream processing (e.g., extraction) of CEPs. This review describes the biochemical features and organization of CEPs and how this fits them for the purpose of protein hydrolysis. It begins with a focus on the genetic organization and expression of CEPs. The catalytic behavior and cleavage specificities of CEPs from various LAB are also discussed. Following this, the extraction and purification of most CEPs reported to date is described. The industrial applications of CEPs in food technology, health promotion, as well as in the growing area of water purification are discussed. Techniques for improving the production and catalytic efficiency of CEPs are also given an important place in this review.

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Section: Applications Of Ceps In Food Technology and Human Healthmentioning

confidence: 99%

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

et al. 2020

Comp Rev Food Sci Food Safe

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“…In this last respect, beneficial dietary habits, which include anti-inflammatory and antioxidant foods, have gained in popularity for the prevention of cardiovascular diseases (CVD). Many experimental studies have documented that small sequence peptides are released during gastrointestinal digestion, food processing, and the microbial proteolysis of proteins [7]. Depending on the sequence of amino acids, these bioactive peptides (BP) can exhibit different biological activities [8], mainly through pathways that are still not clearly understood.…”

Section: Introductionmentioning

confidence: 99%

Multifunctional Peptides from Spanish Dry-Cured Pork Ham: Endothelial Responses and Molecular Modeling Studies

Martínez-Sánchez

Pérez‐Sánchez

Gabaldón

et al. 2019

IJMS

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Food peptides contain a very wide range of diversified structures, which explains their diverse range of functional activities. Proatherogenic endothelium is related to vasoconstriction, inflammation, and oxidative stress. In this line, four synthetic bioactive peptides from dry-cured pork ham, previously identified according to their Angiotensin I Converting Enzyme (ACE) inhibitory capacity and high bioavailability, were tested. Among them, KPVAAP displayed an estimated IC50 of 59.22 µM for human ACE inhibition, and docking simulations demonstrated the consistency of the noncompetitive binding with the protein. The addition of synthetic peptides to human endothelial cells significantly prevents the expression of genes related to endothelial dysfunction and inflammation (eNOS, ICAM-1, VCAM-1, IL-6) and lowers NF-κB activation (all p < 0.05). In silico dockings showed that the four bioactive peptides interact with the regulatory subunit NEMO of the NF-κB transcription factor at the same site as other characterized inhibitors (CC2-LZ region). This is the first study linking experimental and computational approaches that shows NF-κB to be the target of biopeptides of food origin. These multifunctional peptides from dry-cured pork ham make them good candidates for further research into their therapeutic or preventive use to attenuate the inflammatory atherosclerotic process.

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“…Our study reveals that BCH-III was more effective than BCH when a single dose was administered, but both showed a comparable antihypertensive effect by the fourth week of oral administration at the studied concentrations. The effect of the long-term antihypertensive effects has been reported in hemp seed protein, soybean protein hydrolysate, and a permeate fraction of pea protein ( Girigh et al., 2014 , 2016 ; Daliri et al., 2019 ). The GI digestion of BCH was likely to generate active peptides that could be readily absorbed, exerting a comparable effect on BCH-III during the long-term study.…”

Section: Resultsmentioning

confidence: 99%

Production and characterization of chicken blood hydrolysate with antihypertensive properties

et al. 2020

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Chicken blood has limited utilization despite its high protein content. Production of a blood hydrolysate exhibiting angiotensin I-converting enzyme ( ACE )–inhibitory activity would be means of valorizing chicken blood. The optimized conditions used to produce chicken blood corpuscle hydrolysate ( BCH ) by Alcalase were 51.1°C, 4% enzyme, and pH 9.6 for 6 h, resulting in a 35.8% degree of hydrolysis and 37.7% ACE inhibition at a peptide concentration of 0.2 mg/mL. The permeate of a 1-kDa membrane, BCH-III, showed a 2.5-fold increase in ACE inhibition compared with that of BCH. BCH-III was resistant to in vitro gastrointestinal digestion, whereas the BCH digesta exhibited an increased ACE-inhibitory activity after digestion. Both BCH and BCH-III were rich in hydrophobic amino acids. A single administration of BCH and BCH-III to spontaneously hypertensive rats at concentrations of 600 and 100 mg/kg, respectively, lowered the systolic blood pressure by −57.7 and −70.9 mmHg, respectively, 6 h after oral administration compared with the control group. The blood pressure–lowering effect of the 600 mg/kg BCH dose was comparable with that of the 100 mg/kg BCH-III dose after 4 wk of oral administration. Both BCH and BCH-III could be developed for use as nutraceutical products with antihypertensive effects.

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Development of a Soy Protein Hydrolysate with an Antihypertensive Effect

Cited by 54 publications

References 34 publications

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

Cell‐envelope proteinases from lactic acid bacteria: Biochemical features and biotechnological applications

Multifunctional Peptides from Spanish Dry-Cured Pork Ham: Endothelial Responses and Molecular Modeling Studies

Production and characterization of chicken blood hydrolysate with antihypertensive properties

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