Bioactive peptides of whey: obtaining, activity, mechanism of action, and further applications

Olvera-Rosales, Laura Berenice; Cruz‐Guerrero, Alma; García-Garibay, J. M.; Gómez-Ruiz, Lorena; Guzmán-Rodríguez, Francisco; González-Olivares, Luis Guillermo

doi:10.1080/10408398.2022.2079113

Cited by 27 publications

(11 citation statements)

References 310 publications

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“…The antioxidant, antimicrobial, antihypertensive, and immunomodulatory properties of milk-derived bioactive peptides have been extensively reported [ 6 , 7 ], as well as the biological functions of bovine milk lipidomics, related to a lower risk for cardiovascular disease and type 2 diabetes [ 8 ]. The peculiar milk bioactivity is also maintained in dairy products and by-products, as recently reported [ 9 ]. The health properties of milk from Mediterranean buffalo ( Bubalus bubalis ) are further ascribed to its peculiar content in L-carnitine, betaines, and short-chain acyl-carnitines [ 10 , 11 ], which can be improved by innovative breed and breeding techniques [ 12 , 13 ].…”

Section: Introductionmentioning

confidence: 56%

Milk Exosomal miR-27b Worsen Endoplasmic Reticulum Stress Mediated Colorectal Cancer Cell Death

et al. 2022

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The relationship between dietary constituents and the onset and prevention of colorectal cancer (CRC) is constantly growing. Recently, the antineoplastic profiles of milk and whey from Mediterranean buffalo (Bubalus bubalis) have been brought to attention. However, to date, compared to cow milk, the potential health benefits of buffalo milk exosome-miRNA are still little explored. In the present study, we profiled the exosomal miRNA from buffalo milk and investigated the possible anticancer effects in CRC cells, HCT116, and HT-29. Results indicated that buffalo milk exosomes contained higher levels of miR-27b, miR-15b, and miR-148a compared to cow milk. Mimic miR-27b transfection in CRC cells induced higher cytotoxic effects (p < 0.01) compared to miR-15b and miR-148a. Moreover, miR-27b overexpression in HCT116 and HT-29 cells (miR-27b+) induced apoptosis, mitochondrial reactive oxygen species (ROS), and lysosome accumulation. Exposure of miR-27b+ cells to the bioactive 3kDa milk extract aggravated the apoptosis rate (p < 0.01), mitochondrial stress (p < 0.01), and advanced endoplasmic reticulum (ER) stress (p < 0.01), via PERK/IRE1/XBP1 and CHOP protein modulation (p < 0.01). Moreover, GSK2606414, the ER-inhibitor (ER-i), decreased the apoptosis phenomenon and XBP1 and CHOP modulation in miR-27b+ cells treated with milk (p < 0.01 vs. miR-27b++Milk), suggesting the ER stress as a cell-death-aggravating mechanism. These results support the in vitro anticancer activity of 3kDa milk extract and unveil the contribution of miR-27b in the promising beneficial effect of buffalo milk in CRC prevention.

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Section: Introductionmentioning

confidence: 56%

Milk Exosomal miR-27b Worsen Endoplasmic Reticulum Stress Mediated Colorectal Cancer Cell Death

et al. 2022

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“…Enzymatic hydrolysis, which is currently the most commonly used method for the preparation of whey protein peptides, is widely used, and its reaction conditions and processes are easy to control. Bioactive peptides typically consist of 2–20 amino acid residues [ 6 ]. Studies have shown that bioactive peptides derived from whey protein possess numerous beneficial properties, such as hypoglycemic [ 7 ], antioxidant [ 8 ], cholesterol-lowering [ 9 ], antihypertensive [ 10 ], antimicrobial [ 11 ], anti-inflammatory [ 12 ], and antithrombotic [ 13 ] activities, thus promoting human health.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Hydrolysis Optimization of Yak Whey Protein Concentrates and Bioactivity Evaluation of the Ultrafiltered Peptide Fractions

Hao,

Li,

Zhao

et al. 2024

Molecules

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Yak whey protein concentrates (YWPCs) have good functional properties, but there is still a gap in the study of their peptides. In this study, peptides were obtained by enzymatic hydrolysis, and the bioactivity of each ultrafiltration fraction was evaluated using an optimal process. YWPCs were isolated and purified from yak milk as the raw material. Alkaline protease, trypsin, and papain were used to hydrolyze YWPCs. The protease with the highest degree of hydrolysis (DH) and peptide concentration was selected as the most suitable enzyme. The effects of pH, temperature, time, and the enzyme-to-substrate ratio (E/S) on the DH and peptide concentration were investigated, and response surface methodology was utilized to optimize the hydrolysis process. The hydrolysate was separated using ultrafiltration membranes with molecular weight cut-offs of 10 kDa, 5 kDa, 3 kDa, and 1 kDa. The bioactivity of each ultrafiltration component was analyzed, including the inhibition rates of α-amylase and xanthine oxidase (XOD) activities and the scavenging rates of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) cation radicals. The results indicated that alkaline protease was the best enzyme for hydrolyzing YWPCs. The peptide concentration in the YWPC hydrolysate was the highest (17.21 mg/mL) at a pH of 8 and a concentration of 7500 U/g, after 2.5 h at 62 °C. The enzymatic hydrolysate was ultrafiltered to yield four peptide fractions, of which the <1 kDa peptides exhibited the highest α-amylase inhibitory activity (22.06%), XOD inhibitory activity (17.15%), and ABTS cationic free radical scavenging rate (69.55%). This demonstrates the potential of YWPC hydrolyzed peptides for hypoglycemic, uric acid-lowering, and antioxidant applications, providing a theoretical basis for the high-value utilization of YWPCs.

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“…According to numerous studies, whey proteins are frequently a potential source of bioactive peptides, which have beneficial effects on human health [ 4 , 5 ]. However, these sequences need to be released following protein hydrolysis to have a biological impact [ 6 ].…”

Section: Introductionmentioning

confidence: 99%

ACE-Inhibitory Activity of Whey Proteins Fractions Derived of Fermentation by Lacticaseibacillus rhamnosus GG and Streptococcus thermophilus SY-102

Olvera-Rosales

Pérez-Escalante

Castañeda‐Ovando

et al. 2023

Foods

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Many studies have reported the benefits of probiotic microorganisms and the production of angiotensin-converting enzyme (ACE) inhibitors. Determining the proteolytic and ACE inhibition capacities during whey fermentation was the goal of the study. Lacticaseibacillus rhamnosus GG, Streptococcus thermophilus SY-102, and both bacteria together were initially inoculated into whey, reaching an initial concentration of 108 CFU per milliliter in each fermentation system. Through the use of TNBS, SDS-PAGE, and SEC-HPLC methods, the proteolytic profile was examined. An in vitro investigation was performed to test the ACE inhibition capacity. With S. thermophilus, the logarithmic phase of microbial development was shorter than with L. rhamnosus (6 and 12 h, respectively). The logarithmic phase in the co-culture fermentation, however, was extended to 24 h. There were no significant differences in pH between the fermentations. However, the co-culture had a greater concentration of protein hydrolysis (453 ± 0.06 μg/mL), as indicated by the amount of free amino groups. Similarly, this fermentation produced more low molecular weight peptides. The higher inhibition activity, which increased at the conclusion of the fermentation with the co-culture and reached 53.42%, was influenced by the higher peptide synthesis. These findings highlighted the significance of creating useful co-culture products.

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Bioactive peptides of whey: obtaining, activity, mechanism of action, and further applications

Cited by 27 publications

References 310 publications

Milk Exosomal miR-27b Worsen Endoplasmic Reticulum Stress Mediated Colorectal Cancer Cell Death

Milk Exosomal miR-27b Worsen Endoplasmic Reticulum Stress Mediated Colorectal Cancer Cell Death

Enzymatic Hydrolysis Optimization of Yak Whey Protein Concentrates and Bioactivity Evaluation of the Ultrafiltered Peptide Fractions

ACE-Inhibitory Activity of Whey Proteins Fractions Derived of Fermentation by Lacticaseibacillus rhamnosus GG and Streptococcus thermophilus SY-102

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