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Comparative assessment of physicochemical and antioxidative properties of mung bean protein hydrolysates.

ABSTRACT: Two commercial plant proteases namely ficin and bromelain, were acquired to hydrolyze mung bean protein over 300 min hydrolysis, and the physicochemical and antioxidative properties of the obtained hydrolysates were investigated. Bromelain-treated mung bean protein hydrolysates presented a higher degree of hydrolysis in comparison with ficin-treated hydrolysates, further modifying their physicochemical and emulsifying properties. All mung bean protein hydrolysates exhibited 50% scavenging of DPPH radical (IC₅₀) in the concentration range from 8.67 to 16.22 μg mL^-1. Our results also showed that strong metal ion-chelating activity was found in the ficin- (higher activity) and bromelain-treated protein hydrolysates. In addition, oxidative stability of linoleic acid was significantly enhanced by two selected protein hydrolysates, particularly the bromelain-treated hydrolysate with the highest inhibition effect of linoleic acid oxidation (94.55 ± 0.10%). Interestingly, both of these two hydrolysates could effectively retard lipid oxidation of sunflower oil and sunflower oil-in-water emulsion, while the ficin-treated hydrolysate showed slightly better performance. Therefore, mung bean protein hydrolysates showed potential to inhibit lipid oxidation, which could be advantageous in the food industry for producing fortified food.

SUBMITTER: Zheng Z

PROVIDER: S-EPMC9048705 | biostudies-literature |

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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Comparative assessment of physicochemical and antioxidative properties of mung bean protein hydrolysates.

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