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Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

ABSTRACT: SUMMARY Research background Milk protein hydrolysates have received particular attention due to their health-promoting effects. Dromedary milk differs from the milk of other dairy animals in the composition and structure of its protein components, which give it unique properties. The bioactivity and functionality of whole dromedary milk proteins and their enzymatic hydrolysates have not received much attention, hence this study aims to investigate the effect of enzymatic hydrolysis of dromedary milk proteins on their antioxidant activities and functional properties. Experimental approach Dromedary milk proteins were treated using four proteolytic enzymes (pepsin, trypsin, ?-chymotrypsin and papain) and two mixtures of enzymes (pancreatin and pronase). The degree of hydrolysis was measured to verify the hydrolysis of the proteins. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography served to determine the molecular mass distribution of the hydrolysates while reversed phase-high performance liquid chromatography (RP-HPLC) was conducted to explore their hydrophobicity. The antioxidant activities were evaluated using various in vitro tests, including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical scavenging capacities, iron(III) reducing ability and chelating activity. Besides, functional properties such as solubility, foaming and emulsification were assessed. Results and conclusions Dromedary milk protein hydrolysates exhibited different degrees of hydrolysis ranging from 17.69 to 41.86%. Apart from that, the hydrolysates showed different electrophoretic patterns, molecular mass distribution and RP-HPLC profiles demonstrating the heterogeneity of the resulting peptides in terms of molecular mass and polarity. The hydrolysates displayed significantly higher antioxidant capacities than the undigested proteins at all the tested concentrations. Iron(II) chelating activity was the most improved assay after proteolysis and the hydrolysate generated with pancreatin had the highest chelating power. Dromedary milk protein hydrolysates possessed good solubility (>89%). Further, foaming and emulsifying properties of dromedary milk proteins were enhanced after their proteolysis. These interfacial properties were influenced by the enzymes employed during proteolysis. Novelty and scientific contribution Enzymatic hydrolysis of dromedary milk proteins is an effective tool to obtain protein hydrolysates with great antioxidant and functional properties. These results suggest that dromedary milk protein hydrolysates could be used as a natural source of antioxidant peptides to formulate functional foods and nutraceuticals.

SUBMITTER: Oussaief O

PROVIDER: S-EPMC7416125 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

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Project description:BackgroundBioactive peptides can prevent damage associated with oxidative stress in humans when consumed regularly. Recently, peptides have attracted immense interest because of their beneficial functional properties, safety and little or no side effects when used at high concentration. Most antioxidant peptides are small in size, less than 1 kDa, and contains a high proportion of hydrophobic amino acid. Particularly, tyrosine, leucine, alanine, isoleucine, valine, lysine, phenyalanine, cysteine, methionine and histidine in peptide chain exhibited high antioxidant activity. Mungbean meal protein (MMP) is highly abundant in hydrophobic amino acids. It indicated that MMP might be a good source of antioxidants. Therefore, the objectives were to optimize the conditions used to generate mungbean meal protein hydrolysate (MMPH) with antioxidant activity from bromelain and to investigate the antioxidant activities of different molecular weight (MW) peptide fraction.MethodsResponse Surface Methodology (RSM) was used for screening of the optimal conditions to produce MMPH. After that MMPH was fractionated using ultrafiltration membranes with different MW distributions. Crude-MMPH and four fractions were investigated for five antioxidant activities: 2,2,1-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, superoxide, ferric reducing antioxidant power (FRAP) and metal ion chelation activity.ResultsThe optimal condition to produce the MMPH was 15% (w/w) of bromelain and hydrolysis time for 12 h which showed the greatest DPPH and ABTS radical scavenging activity. After mungbean protein from optimal condition was separated based on different molecular weight, the DPPH radical scavenging activity was the highest for the F4 (less than 1 kDa) peptide fraction. Metal ion chelating activity was generally weak, except for the F4 that had a value of 43.94% at a protein concentration of 5 mg/mL. The F4 also exhibited high hydroxyl and superoxide activities (54 and 65.1%), but moderate activity for ferric reducing antioxidant power (0.102 mmole Fe2+/g protein) compared to other peptide fractions and crude-MMPH. Molecular weight and amino acid were the main factors that determined the antioxidant activities of these peptide fractions. Results indicated that F4 had strong antioxidant potentials.DiscussionThe lowest MW fraction (less than 1 kDa) contributed to the highest DPPH, superoxide, hydroxyl and metal chelation activity because influence of low MW and high content of hydrophobic amino acid in peptide chain. Results from this study indicated that MMPH peptides donate protons to free radicals because they had significantly high DPPH value compared to superoxide, hydroxyl and FRAP, which reactions were electron donation. Moreover, MMPH peptides had the ability to inhibit transition metal ions because of highly abundant glutamic acid and aspartic acid in peptide chain.

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Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

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