Whey Peptides Research Articles

Digestion of whey peptide induces antioxidant and anti-inflammatory bioactivity on glial cells: Sequences identification and structural activity analysis

Whey derived peptides have shown potential activity improving brain function in pathological condition. However, there is little information about their mechanism of action on glial cells, which have important immune functions in brain. Astrocytes and microglia are essential in inflammatory and oxidative defense that take place in neurodegenerative disease. In this work we evaluate antioxidant and anti-inflammatory potential bioactivity of whey peptide in glial cells. Peptides were formed during simulated gastrointestinal digestion (Infogest protocol), and low molecular weight (<5kDA) peptides (WPHf) attenuated reactive oxygen species (ROS) production induced by hydrogen peroxide stimulus in both cells in dose-dependent manner. WPHf induced an increase in the antioxidant glutathione (GSH) content and prevented GSH reduction induced by lipopolysaccharides (LPS) stimulus in astrocytes cells in a cell specific form. An increase in cytokine mRNA expression (TNFα and IL6) and nitric oxide secretion induced by LPS was attenuated by WPHf pre-treatment in both cells. The inflammatory pathway was dependent on NFκB activation. Bioactive peptide ranking analysis showed positive correlation with hydrophobicity and negative correlation with high molecular weights. The sequence identification revealed 19 peptides cross-referred with bioactive database. Whey peptides were rich in leucine, valine and tyrosine in the C-terminal region and lysine in the N-terminal region. The anti-inflammatory and antioxidant potential of whey peptides were assessed in glia cells and its mechanisms of action were related, such as modulation of antioxidant enzymes and anti-inflammatory pathways. Features of the peptide structure, such as molecular size, hydrophobicity and types of amino acids present in the terminal region are associated to bioactivity.

Evaluation of the Improvement Effect of Whey Protein Poly-Peptides on Quality Characteristics of Repeated Freeze–Thawed Spanish Mackerel Surimi Balls

This investigation aimed to assess the effects of whey protein hydrolysate (WPH) on the oxidative stability of protein and the ability of Scomberomorus niphoniu surimi balls to retain water after repeated freeze-thaw (F-T) cycles. Ten percent natural whey peptides (NWP), 5% WPH, 10% WPH, 15% WPH, 0.02% butyl hydroxyl anisole (BHA), and a control group that did not receive any treatment were the six groups that were employed in the experiment. The cooking loss, water retention, total sulfhydryl content, and carbonyl content of each group were all measured. Notably, it was found that the surimi balls’ capacity to hold onto water and fend off oxidation was enhanced in a dose-dependent manner by the addition of WPH. Furthermore, the results showed that the 15% WPH added to the surimi balls effectively decreased protein oxidation in the F–T cycles and ameliorated the texture deterioration of surimi balls induced by repeated F–T, laying a theoretical foundation for the industrial application of WPH in surimi products.

Exploring peptidomes of by-products generated during chhurpi production using Lactobacillus delbrueckii WS4 for identification of novel bioactive peptides.

The considerable value of whey is evident from its significant potential applications and contributions to the functional food and nutraceutical market. The by-products were individually obtained during functional chhurpi and novel soy chhurpi cheese production using defined lactic acid bacterial strains of Sikkim Himalaya's traditional chhurpi. Hydrolysis of substrate proteins by starter proteinases resulted in a comparable peptide content in whey and soy whey which was associated with antioxidant and ACE inhibition potential. Peptidome analysis of Lactobacillus delbrueckii WS4 whey and soy whey revealed the presence of several bioactive peptides including the multifunctional peptides PVVVPPFLQPE and YQEPVLGPVRGPFPIIV. In silico analyses predicted the antihypertensive potential of whey and soy whey peptides with strong binding affinity for ACE active sites. QSAR models predicted the highest ACE inhibition potential (IC50) for the β-casein-derived decapeptide PVRGPFPIIV (0.95 μM) and the Kunitz trypsin inhibitor protein-derived nonapeptide KNKPLVVQF (16.64 μM). Chhurpi whey and soy whey can be explored as a valuable source of diverse and novel bioactive peptides for applications in designer functional foods development.

Application of antioxidant peptides derived from goat milk in ginger coffee formulation

Peptides can be obtained from the degradation of goat milk protein by enzymatic hydrolysis method using food-grade papain enzyme. These peptides have antioxidant activity that can be applied to beverage formulations. This study aimed to characterize antioxidative peptides from whey and goat milk and to develop a ginger coffee drink formulation with antioxidant peptides. Protein hydrolysis was performed for 0, 15, and 30 mins and the highest degree of hydrolysis was obtained from protein samples which were hydrolyzed for 15 mins. The whey hydrolysate 15 mins had a protein concentration of 0.54±0.07 mg/mL and one protein band of 17 kDa. Goat milk peptides had a protein concentration of 1.71±0.00 mg/mL and one protein band of 15 kDa. This sample also has the highest antioxidant activity, where Whey peptides had an antioxidant activity of 79.98±0.86% while goat's milk peptides 94.97±0.44%. These two peptides were applied to ginger coffee drink formulation. The formulations with the highest antioxidant activity were ginger coffee with goat milk and whey peptides in a ratio of 4:1 (90.15±1.02%) and ginger coffee with goat milk (85.23±1.15%). Based on results from the organoleptic test, these two formulations were also acceptable to panellists in terms of taste, overall properties, and interest.

Entrapment of curcumin in hydrogels of whey peptides and its release during static in vitro gastrointestinal digestion

The suitability of a whey peptide hydrogel for entrapping curcumin compared with a whey protein isolate (WPI) gel was investigated. In addition, the release of curcumin entrapped in the peptide and protein gels was evaluated during static in vitro gastrointestinal digestion. The peptide hydrogel showed a 91% entrapment efficiency of curcumin compared with 99.9% for the WPI gel and at the end of intestinal digestion curcumin retention was close to 98% in the peptide hydrogel, whereas it was only 90% for the WPI gel. The preservation of the gel microstructure and, consequently, peptide-curcumin hydrophobic interactions during intestinal digestion could explain why curcumin release from the peptide hydrogel was lower than from the WPI gel. This work provides innovative results regarding the potential of using food-derived peptide hydrogels as an entrapment system for curcumin and its preservation during digestive conditions.

Effects of Whey Peptides on the Quality of Pork Ball Preprepared Dishes during Repeated Freezing-Thawing.

This study evaluated the effect of FI (Fraction I, molecular weight < 1 kDa), which is separated from natural whey protein, on the antioxidant activity, sensory quality, color, texture characteristics, and microbial growth of pork balls during repeated freeze-thaw cycles (F-T cycles). The results indicated that pork balls mixed with FI significantly improved in quality after repeating the F-T cycle, especially with the addition of 10% FI. The quality was improved significantly after repeated F-T cycles by adding 10% FI, and the antioxidant activity after seven F-T cycles decreased by 40.78%, a similar result to that obtained with the addition of 0.02% BHA. In addition, FI effectively reduced the sensory damage of pork balls caused by repeated freezing-thawing and also significantly inhibited the growth of microorganisms. In summary, FI not only has excellent antioxidant capacity under repeated freeze-thaw conditions but also has significant antibacterial and quality preservation effects and is expected to be quantified as a kind of natural food additive with antibacterial and antioxidant properties. This paper not only explores the effect of FI on the quality characteristics of frozen and thawed pork balls in prepared dishes but also provides a theoretical basis for the application of whey polypeptides in prepared meat.

In Silico Strategies to Predict Anti-aging Features of Whey Peptides.

We have analysed the in silico potential of bioactive peptides from cheese whey, the most relevant by-product from the dairy industry, to bind into the active site of collagenase and elastase. The peptides generated from the hydrolysis of bovine β-lactoglobulin with three proteases (trypsin, chymotrypsin, and subtilisin) were docked onto collagenase and elastase by molecular docking. The interaction models were ranked according to their free binding energy using molecular dynamics simulations, which showed that most complexes presented favourable interactions. Interactions with elastase had significantly lower binding energies than those with collagenase. Regarding the interaction site, it was found that four bioactive peptides were positioned in collagenase's active site, while six were found in elastase's active site. Among these, the most we have found one promising collagen-binding peptide produced by chymotrypsin and two for elastase, produced by subtilisin and chymotrypsin. These in silico results can be used as a tool for designing further experiments aiming at testing the in vitro potential of the peptides found in this work.

Influence of Complexation with β- and γ-Cyclodextrin on Bioactivity of Whey and Colostrum Peptides.

Dairy protein hydrolysates possess a broad spectrum of bioactivity and hypoallergenic properties, as well as pronounced bitter taste. The bitterness is reduced by complexing the proteolysis products with cyclodextrins (CDs), and it is also important to study the bioactivity of the peptides in inclusion complexes. Hydrolysates of whey and colostrum proteins with extensive hydrolysis degree and their complexes with β/γ-CD were obtained in the present study, and comprehensive comparative analysis of the experimental samples was performed. The interaction of CD with peptides was confirmed via different methods. Bioactivity of the initial hydrolysates and their complexes were evaluated. Antioxidant activity (AOA) was determined by fluorescence reduction of fluorescein in the Fenton system. Antigenic properties were studied by competitive enzyme immunoassay. Antimutagenic effect was estimated in the Ames test. According to the experimental data, a 2.17/2.78-fold and 1.45/2.14-fold increase in the AOA was found in the β/γ-CD interaction with whey and colostrum hydrolysates, respectively. A 5.6/5.3-fold decrease in the antigenicity of whey peptides in complex with β/γ-CD was detected, while the antimutagenic effect in the host-guest systems was comparable to the initial hydrolysates. Thus, bioactive CD complexes with dairy peptides were obtained. Complexes are applicable as a component of specialized foods (sports, diet).

Antitumor activity of a whey peptide-based enteral diet in C26 colon tumor-bearing mice.

The antitumor effects of a whey peptide-based enteral diet, whose main components are whey peptides and yogurt fermented by Lactobacillus delbureckii subsp. bulgaricus 2038 and Streptococcus thermophilus 1131, were investigated in mice. Our results indicated that the tumor weight in C26 carcinoma-transplanted mice was significantly smaller at day 16 post-implantation in the whey peptide-based enteral diet group (1.36±0.54g) than in the control group (1.83±0.89g) (p <0.05). The whey peptide-based enteral diet group exhibited higher tumor cell apoptosis, lower cell proliferation, and inactive angiogenesis indicating by higher degree of TUNEL, lower positive rates of Ki-67, VEGF, and CD34 than control group. It also attenuated inflammatory cell infiltration of spleen and liver as indicated by the decreased spleen index (10.89±2.06vs. 12.85±2.92, p<0.05) and increased liver index (58.09±11.37vs. 53.19±6.67, p<0.05) in the whey peptide-based enteral diet group than the control diet group. These results proved the inhibitory effect of the whey peptide-based enteral diet on tumor growth, which might be attributed to the whey peptides component. PRACTICAL APPLICATION: A whey peptide-based enteral diet (MEIN® ), containing cheese whey and multiple nutrients, was selected to verify the anti-tumor effect by animal experiments. The tumor weight growth, tumor cell proliferation, inflammatory cell infiltration of spleen and liver in tumor model mice was significantly attenuated by the whey peptide-based enteral diet, that might be attributed to its whey peptides component. These results provided an additive direction for cancer therapy and need a further study including clinical trials.

Digestion-resistant whey peptides promote antioxidant effect on Caco-2 cells

Enteric endothelial cells are the first structure to come in contact with digested food and may suffer oxidative damage by innumerous exogenous factors. Although peptides derived from whey digestion have presented antioxidant potential, little is known regarding antioxidant pathways activation in Caco-2 cell line model. Hence, we evaluated the ability to form whey peptides resistant to simulated gastrointestinal digestive processes, with potential antioxidant activity on gastrointestinal cells and associated with sequence structure and activity. Using the INFOGEST method of simulated static digestion, we achieved 35.2% proteolysis, with formation of peptides of low molecular mass (<600 Da) evaluated by FPLC. The digestion-resistant peptides showed a high proportion of hydrophobic and acidic amino acids, but with average surface hydrophobicity. We identified 24 peptide sequences, mainly originated from β-lactoglobulin, that exhibit various bioactivities. Structurally, the sequenced peptides predominantly contained the amino acids lysine and valine in the N-terminal region, and tyrosine in the C-terminal region, which are known to exhibit antioxidant properties. The antioxidant activity of the peptide digests was on average twice as potent as that of the protein isolates for the same concentration, as evaluated by ABTS, DPPH and ORAC. Evaluation of biological activity in Caco-2 intestinal cells, stimulated with hydrogen peroxide, showed that they attenuated the production of reactive oxygen species and prevented GSH reduction and SOD activity increase. Caco-2 cells were not responsive to nitric oxide secretion. This study suggests that whey peptides formed during gastric digestion exhibit biological antioxidant activity, without the need for previously hydrolysis with exogenous enzymes for supplement application. The study’s primary contribution was demonstrating the antioxidant activity of whey peptides in maintaining the gastrointestinal epithelial cells, potentially preventing oxidative stress that affects the digestive system.

Chitosan complexes with amino acids and whey peptides: Sensory and antioxidant properties

Chitosan reacts with amino acids and hydrolyzed whey proteins to produce biologically active complexes that can be used in functional foods. The research objective was to obtain chitosan biocomposites with peptides and amino acids with improved antioxidant and sensory properties. &#x0D; The research featured biocomposites of chitosan and succinylated chitosan with whey peptides and amino acids. The methods of pH metry and spectrophotometry were employed to study the interaction parameters between polysaccharides and peptides, while colorimetry and spectrophotometry served to describe the amino acids content. The antiradical effect was determined by the method of fluorescence recovery. Pure compounds and their complexes underwent a sensory evaluation for bitterness. &#x0D; Chitosan and succinylated chitosan formed complexes with whey peptides and such proteinogenic amino acids as arginine, valine, leucine, methionine, and tryptophan. The equimolar binding of tryptophan, leucine, and valine occurred in an aqueous chitosan solution (in terms of glucosamine). Methionine appeared to be the least effective in chitosan interaction, while arginine failed to complex both with chitosan and succinylated chitosan. Chitosan and succinylated chitosan biocomposites with peptides and leucine, methionine, and valine proved to be less bitter that the original substances. The samples with arginine maintained the same sensory properties. Chitosan complexes with tryptophan and peptides increased their antioxidant activity by 1.7 and 2.0 times, respectively, while their succinylated chitosan complexes demonstrated a 1.5 fold increase.&#x0D; Chitosan and succinylated chitosan biocomplexes with tryptophan and whey protein peptides had excellent antioxidant and sensory properties. However, chitosan proved more effective than succinylated chitosan, probably, because it was richer in protonated amino groups, which interacted with negatively charged amino acids groups.

In vitro biosafety and bioactivity assessment of the goat milk protein derived hydrolysates peptides

AbstractGoat milk and protein hydrolysate peptides have generated significant interest due to their diverse range of biological functions. To produce these peptides, casein (CP), and whey proteins (WP) were partially purified from goat milk and subsequently hydrolyzed with gastrointestinal endopeptidases such as pepsin, trypsin, and α‐chymotrypsin based on in silico selection to achieve gastrointestinal stable peptides. The hydrolysates were characterized using various techniques, including zeta sizer, polydispersity index (PDI), zeta potential, and reverse‐phase high‐performance liquid chromatography (RP‐HPLC). The resulting peptides were then purified using RP‐HPLC. To assess cytotoxicity, an MTT (3‐[4, 5‐dimethylthiazol‐2‐yl]‐2, 5‐diphenyl tetrazolium bromide) assay was performed with fluorescence microscopy. Finally, cytokine levels were determined using enzyme‐linked immunosorbent assay (ELISA). In comparison to WP and CP, the casein protein hydrolysates (CPH) and whey protein hydrolysates (WPH) peptides average particle size and PDI were decreased. The zeta potential of casein and whey peptides hydrolysates there were no differences. The RP‐HPLC analysis revealed the production of peptides through the hydrolysis of CP and WP. These hydrolysates peptides were found to possess diverse biological activities, as evidenced by their significant inhibition of α‐amylase, pancreatic lipase (PL), and angiotensin‐converting enzyme (ACE), as well as their antibacterial properties against selected pathogens. Further investigations were carried out to understand the mode of action of these peptides using fluorescence and scanning electron microscope (SEM) microscopy. This study provides the first evidence of gastrointestinal stable peptides derived from goat milk with inhibitory activity against α‐amylase, PL, and ACE, as well as antibacterial properties against specific pathogens. Additionally, the peptides demonstrated significant cytokine inhibition and low toxicity toward the HT‐29 cell line. This study strongly suggests that the biologically active peptides responsible for the health‐related bioactive properties described here, which are considered functional and nutraceutical ingredients, should be identified and validated in subsequent research, particularly the most effective hydrolysate peptides derived from goat milk protein. Goat milk is widely recognized as an excellent source of milk protein. In this study, bioactive peptides were produced using casein and whey proteins from goat milk, which exhibited inhibitory activity against angiotensin converting enzyme, α‐amylase, and pancreatic lipase, as well as antibacterial properties. Goat milk protein is a promising source for developing high‐quality protein products with excellent safety standards that have potential applications in the pharmaceutical and food industries.

The trophic effects of an enteral formula containing whey peptides on the intestinal tract

牛乳由来のホエイタンパク質は消化吸収が早く,分岐鎖アミノ酸などの必須アミノ酸を豊富に含むことから栄養学的に優れたタンパク質源である.近年，われわれはホエイタンパク質およびその加水分解ペプチドが抗炎症効果を有することを見い出した.そこでこのホエイタンパク質の栄養学的優位性と生体調節作用に着目し，ホエイペプチド配合流動食MHN‐02を開発し，その有用性をさまざまな病態モデルにより評価してきた.その中で，MHN‐02はインドメタシン誘発ラット小腸障害モデルにおいて，腸間膜リンパ節および肝臓へのバクテリアルトランスロケーションを抑制することを明らかにし，その効果はMHN‐02の小腸粘膜の保護作用が関連することを組織学的解析から示した.さらにこのような腸管保護作用を有するMHN‐02は抗がん剤5‐フルオロウラシルの副作用である下痢の発生を遅延させ，体重を維持することも明らかにした.以上のことからホエイペプチドを配合したMHN‐02は優れた栄養組成と腸管機能の維持を通して，各種病態において治療に伴う副作用を軽減し，栄養状態を維持することによって，治療効果の向上に貢献することが期待できる.

Oral acetylated whey peptides (AWP) as a potent antioxidant, anti-inflammatory, and chelating agent in iron-overloaded rats' spleen

Excessive iron accumulation is highly toxic to various tissues. Acetylated whey peptides (AWP) obtained from bovine milk have a powerful iron chelating and immunomodulation effect. This study was performed on iron overload (IO)-induced rats' spleen model and announced that AWP can act as a potent prophylactic, natural, affordable, oral and safe iron chelator and can be used as an alternative to the current synthetic drugs. Moreover, it can alleviate oxidative stress and downregulate the proinflammatory markers. The results showed that AWP significantly decreased serum iron, splenic ferritin, oxidative stress markers (ROS, iNOS, and HO-1), and inflammatory markers (IL-6, IL-1β, and NF-κB). Histopathological examination declared that AWP reduced splenic iron deposition and improved histopathological changes in iron-overloaded rats. Immunohistochemical examination showed a significant decrease in macrophage markers (CD68 and CD163) expressions. The efficacy of AWP was compared to that of N-Acetyl-l-cysteine (NAC) and both of them showed no significant difference.

Hypoxia-Driven Changes in a Human Intestinal Organoid Model and the Protective Effects of Hydrolyzed Whey.

Many whey proteins, peptides and protein-derived amino acids have been suggested to improve gut health through their anti-oxidant, anti-microbial, barrier-protective and immune-modulating effects. Interestingly, although the degree of hydrolysis influences peptide composition and, thereby, biological function, this important aspect is often overlooked. In the current study, we aimed to investigate the effects of whey protein fractions with different degrees of enzymatic hydrolysis on the intestinal epithelium in health and disease with a novel 2D human intestinal organoid (HIO) monolayer model. In addition, we aimed to assess the anti-microbial activity and immune effects of the whey protein fractions. Human intestinal organoids were cultured from adult small intestines, and a model enabling apical administration of nutritional components during hypoxia-induced intestinal inflammation and normoxia (control) in crypt-like and villus-like HIO was established. Subsequently, the potential beneficial effects of whey protein isolate (WPI) and two whey protein hydrolysates with a 27.7% degree of hydrolysis (DH28) and a 50.9% degree of hydrolysis (DH51) were assessed. In addition, possible immune modulatory effects on human peripheral immune cells and anti-microbial activity on four microbial strains of the whey protein fractions were investigated. Exposure to DH28 prevented paracellular barrier loss of crypt-like HIO following hypoxia-induced intestinal inflammation with a concomitant decrease in hypoxia inducible factor 1 alpha (HIF1α) mRNA expression. WPI increased Treg numbers and Treg expression of cluster of differentiation 25 (CD25) and CD69 and reduced CD4+ T cell proliferation, whereas no anti-microbial effects were observed. The observed biological effects were differentially mediated by diverse whey protein fractions, indicating that (degree of) hydrolysis influences their biological effects. Moreover, these new insights may provide opportunities to improve immune tolerance and promote intestinal health.

Impact of casein-to-whey protein ratio on gastric emptying, proteolysis, and peptidome profile of fermented milk during in vitro dynamic gastrointestinal digestion in preschool children

The effects of casein-to-whey ratios (i.e., 4:1, 2:1, 1:1, 1:1.5) in fermented milk on gastric emptying, proteolysis and intestinal peptidome were investigated using an in vitro dynamic stomach-intestine system mimicking preschool children digestion. The gastric emptying rate varied insignificantly among the milk samples. After 120 min digestion, the protein digestibility was found in the range of 73.3–93.5 %, with the highest extent of proteolysis observed at a casein-to-whey ratio of 2:1 due to the fewest gastric protein aggregates and relatively abundant caseins. Intestinal peptides derived from caseins or whey proteins showed a positive correlation with their parent protein content. The most abundant bioactive whey peptides were found at casein-to-whey ratio of 1:1.5 after intestinal digestion. These findings demonstrated the importance of protein compositions in fermented milk on the gastrointestinal proteolysis and peptide release in vitro. This will be meaningful for future development of milk products that are more suitable for children.

Donkey whey protein and peptides regulate gut microbiota community and physiological functions of D-galactose-induced aging mice.

The prolongation of life span has attracted more and more attention in the current world. Gut microbiota is considered one of the most critical elements and is essential in regulating life span and quality. The effects of donkey whey protein (DWP) and donkey whey hydrolysate (DWPP) on physiological functions and gut microbiota of D-galactose-induced aging mice were investigated to find new strategies for resisting aging. Our results showed that DWP and DWPP could increase the body weight gain velocity, superoxide dismutase (SOD) activity, and thymus index, whereas decrease the level of reactive oxygen species (ROS) and malondialdehyde (MDA), and improve the aging of the body in the liver congestion, oozy draw focal sclerosis of chronic inflammation. The effects of medium and high concentrations of DWP and low and medium concentrations of DWPP were the same as the vitamin C (Vc)-positive control group. It was found that both DWP and DWPP could change α-diversity; the relative abundance of Lactobacillus increased, whereas the relative abundance of Helicobacter and Stenotrophomonas decreased after being treated with DWP and DWPP. The correlation between intestinal microflora and physiological indexes showed that chao1, ACE, and observed species indexes in the α index were positively correlated with weight gain velocity, SOD activity, and thymus index. The relative abundance of Lactobacillus was positively correlated with SOD and thymus index but negatively correlated with MDA. The relative abundance of Stenotrophomonas was opposite to that of Lactobacillus. The Anaerobiospirillum, Fusobacterium, and Dubosiella had a significant positive correlation with the weight gain velocity. The study provided a deeper more profound understanding of the potential use of DWP and DWPP in senescence delays.

Мультикомпонентные композиты нанокомплексов циклодекстрина с биологически активными веществами для функциональных продуктов питания

Enzymatic protein hydrolysates of milk are used as a protein component of functional foods intended for children, athletes, and senior citizens. They are easy to absorb and possess hypoallergenic, antioxidant, antimicrobial, and antimutagenic properties. However, the peptides in their composition have a bitter taste, which limits the use of milk protein hydrolysates in food industry. Functional foods are often fortified with fat-soluble vitamins and other hydrophobic ingredients. They require multicomponent compositions that contain both hydrophilic and hydrophobic compounds. Complexes of β-cyclodextrins with peptides of whey protein hydrolyzates and fat-soluble vitamins can solve this problem. &#x0D; The present research featured nanocomplexes of β-cyclodextrins with whey peptides and their multicomponent mixes with vitamins D3 and A. The methodology involved HPLC-MS, electrophoresis, thermogravimetry, and fluorimetry. &#x0D; The obtained clathrates were used to develop new multicomponent compositions for functional nutrition. The article introduces a new production method for hypoallergenic peptide fractions with a molecular weight of 300–1500 Da from enzymatic whey protein hydrolyzates. The obtained peptides contained 6–14 amino acid residues and demonstrated hypoallergenic properties because they contained no antigenic determinants capable of causing IgE synthesis. The complexes of inclusion contained hydrolyzate peptides of dairy proteins and fat-soluble vitamins A and D3. The research revealed some antioxidant and antimutagenic properties, as well as the toxicological and hygienic profile of the clathrates. The resulting peptide clathrates had a less bitter taste. The inclusion complexes of fat-soluble vitamins D3:β-cyclodextrins, and A:β-cyclodextrins could be converted from an olive oil solution into a soluble powder. 100 g of the multicomponent composite contained 47.0 g of whey protein hydrolyzate of low molecular weight fraction peptides, 1.06 mg of vitamin D3 (42 500 IU), 3.44 mg of vitamin A (10 000 IU), and 1.54 g of olive oil. The article also describes the structural and functional properties of the inclusion complexes. Nanocomplexes of whey protein hydrolyzate of low molecular weight fraction peptides:β-cyclodextrins, D3:β-cyclodextrins, and A:β-cyclodextrins and their multicomponent composite were tested for toxicological and hygienic properties using Tetrahymena pyriformis. They appeared to belong to the 5th hazard class in terms of the average lethal dose (non-hazardous substances). &#x0D; The obtained powder forms of fat-soluble vitamins and peptides are easily dosed and can be used to design new functional foods.

Antiproliferative Activity of Whey and Casein Bioactive Peptides on Breast Cancer: An In Vitro and In Silico Study

Antiproliferative Activity of Whey and Casein Bioactive Peptides on Breast Cancer: An In Vitro and In Silico Study

Whey protein-derived peptides: The impact of chicken pepsin hydrolysis upon whey proteins concentrate on their biological and technological properties

Whey proteins concentrate (WPC) was hydrolysed by chicken pepsin extract (CPE) compared with commercial porcine pepsin (PP), and the impact on biological (antioxidant) and technological properties (solubility, emulsifying activity index (EAI) and foaming activity (FA)) was studied. The results showed no significant differences between degree of hydrolysis (DH) values for both enzymes and ratios E/S tested. Total degradation of α-lactalbumin (α-La) was observed, while not for β-lactoglobulin (β-Lg). The hydrolysates produced by both enzymes had enhanced ABTS and ORAC antioxidant capacity. The hydrolysate obtained with both enzymes that had the maximum DH and antioxidant activity, also exhibited improvement of solubility at the pH range of 3–8. In contrast, EAI and FA of PP hydrolysates were enhanced at some pH points only. The obtained results with CPE are very promising and suggest that they could be suitable for application in functional food as natural ingredients.