Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides

Chunkao, Siriporn; Youravong, Wirote; Yupanqui, Chutha Takahashi; Alashi, Adeola M.; Aluko, Rotimi E.

doi:10.3390/foods9101406

Cited by 24 publications

(16 citation statements)

References 49 publications

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“…Bioactive peptides normally contain 2–20 amino acid residues with low molecular weight and have a variety of biological activities depending on the type of amino acid, molecular size, and sequence [ 8 , 9 ]. The antioxidant activities of several plant protein-derived peptides have been determined including chickpea [ 10 , 11 ], wheat [ 12 ], barley [ 13 ], soybean [ 14 ], corn [ 15 ], rapeseed [ 16 , 17 ], and mung bean [ 18 , 19 , 20 , 21 ].…”

Section: Introductionmentioning

confidence: 99%

Functional Characterization of Mung Bean Meal Protein-Derived Antioxidant Peptides

et al. 2021

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The aim of this work was to characterize the antioxidant properties of some of the peptides present in bromelain mung bean meal protein hydrolysate (MMPH). The MMPH was subjected to two rounds of bioassay-guided reversed-phase HPLC separation followed by peptide identification in the most potent fractions using tandem mass spectrometry. Twelve antioxidant peptides, namely, HC, CGN, LAN, CTN, LAF, CSGD, MMGW, QFAAD, ERF, EYW, FLQL, and QFAW were identified and assayed for antioxidant properties. CTN, HC, CGN, and CSGD were the most potent (p < 0.05) DPPH radical scavengers with EC50 values of 0.30, 0.29, 0.28, and 0.30 mg/mL, respectively, which are lower than the 0.03 mg/mL obtained for reduced glutathione (GSH). CTN, HC, CGN, and CSGD exhibited the most potent (p < 0.05) scavenging activities against hydroxyl and superoxide radicals with EC50 values that are similar to those of GSH. The cysteine-containing peptides also had stronger ferric reducing antioxidant power and metal chelation activity than peptides devoid of cysteine. In contrast, MMGW, ERF, and EYW had poor radical scavenging and metal chelation activities. We conclude that the availability of the sulfhydryl group may have enhanced antioxidant potency while the presence of bulky groups such phenylalanine and tryptophan had an opposite effect.

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Section: Introductionmentioning

confidence: 99%

Functional Characterization of Mung Bean Meal Protein-Derived Antioxidant Peptides

et al. 2021

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“…Another study also confirmed the potential of mung bean protein-derived peptides for iron-binding capacity [143]. Using an enzymatic membrane reactor, the mung protein hydrolysate was prepared, and further peptide separation was carried out by anion-exchange chromatography and reverse-phase HPLC.…”

Section: Mineral-binding Peptidesmentioning

confidence: 71%

“…Wheat germ Pentapeptide FVDVT Calcium-binding property [137] Walnut flake VEDELVAVV and LAGNPDDEFRPQ Iron-chelating peptides [141] Mung bean HADAD, AIVIL, and LLLGI Calcium-binding capability [142] Mung bean PAIDL Iron-binding capacity [143]…”

Section: Seeds Bioactive Peptides Activities Referencesmentioning

confidence: 99%

Production, Purification, and Potential Health Applications of Edible Seeds’ Bioactive Peptides: A Concise Review

Samtiya

Acharya²,

Pandey³

et al. 2021

Foods

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Edible seeds play a significant role in contributing essential nutritional needs and impart several health benefits to improve the quality of human life. Previous literature evidence has confirmed that edible seed proteins, their enzymatic hydrolysates, and bioactive peptides (BAPs) have proven and potential attributes to ameliorate numerous chronic disorders through the modulation of activities of several molecular markers. Edible seed-derived proteins and peptides have gained much interest from researchers worldwide as ingredients to formulate therapeutic functional foods and nutraceuticals. In this review, four main methods are discussed (enzymatic hydrolysis, gastrointestinal digestion, fermentation, and genetic engineering) that are used for the production of BAPs, including their purification and characterization. This article’s main aim is to provide current knowledge regarding several health-promoting properties of edible seed BAPs in terms of antihypertensive, anti-cancer, antioxidative, anti-inflammatory, and hypoglycemic activities.

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“…In this study, hydrothermal treatment (temperature, time, and moisture content) was found to significantly affect the gel properties of MBPs because it disrupts the MBP structure, thereby exposing hydrophobic groups and intensifying protein interactions ( 28 , 29 ). Chunkao et al demonstrated that 85°C is the denaturation temperature of MBPs and that denatured MBPs expose more hydrophobic regions and sulfhydryl groups, resulting in high gel strength ( 30 ). The formation to stabilization stages of the MBP gels were discovered to occur at 85°C for 0–60 min.…”

Section: Discussionmentioning

confidence: 99%

Hydrothermal-induced changes in the gel properties of Mung bean proteins and their effect on the cooking quality of developed compound noodles

et al. 2022

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Mung bean proteins (MBPs) are highly nutritious food ingredients, but their lack of gluten limits their use in staple foods such as noodles. In this study, MBPs were modified by hydrothermal treatment, and their gel properties and the major structural changes were analyzed at different heating temperatures (25, 65, 75, 85, 95, and 105°C), moisture contents (0, 15, 20, 25, 30, and 35%), and hydrothermal treatment times (0, 15, 30, 45, 60, and 75 min). Thereafter, the modified MBPs (MMBPs) were added to wheat noodles at substitution levels of 3, 6, and 9% to evaluate their effect on the quality of the noodles. The results showed that the hydrothermal treatment significantly improved the gel properties and water absorption capacity of the MBPs and slightly increased their disulfide bond content. When MBPs with a 25% moisture content were heated at 85°C for 60 min, their gel properties notably improved, and their structural changes were maximal. The structural changes revealed that the MBP molecule formed a macromolecular polymer because a significant protein band appeared at about 66.2 kDa. Secondary structure and microstructure analyses revealed that the MBP structure was significantly damaged and that the β-sheet structure increased because of changes in the degree of aggregation between the protein molecules. Compared to the untreated MBPs, the MMBPs significantly improved the cooking quality and texture properties of the noodles, and the addition amount reached more than 6%, whereas that of the untreated MBPs was less than 3%. At this time, the cooking loss and the broken rate of the untreated MBPs group were about 2 times higher than that of the 6% MMBP-treated group. An analysis of changes in the water distribution, rheological properties, and microstructure revealed that intermolecular cross-linking occurred between the MMBPs and wheat dough, which improved the quality of the MMBP-treated noodles. The findings demonstrated that the MMBPs obtained by hydrothermal treatment had a positive effect on the wheat dough properties and noodle quality. These results provide a technical foundation for incorporating novel protein supplements into staple foods.

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Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides

Cited by 24 publications

References 49 publications

Functional Characterization of Mung Bean Meal Protein-Derived Antioxidant Peptides

Functional Characterization of Mung Bean Meal Protein-Derived Antioxidant Peptides

Production, Purification, and Potential Health Applications of Edible Seeds’ Bioactive Peptides: A Concise Review

Hydrothermal-induced changes in the gel properties of Mung bean proteins and their effect on the cooking quality of developed compound noodles

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