Structural and functional characterization of calcium and iron-binding peptides from mung bean protein hydrolysate

Budseekoad, Siriporn; Yupanqui, Chutha Takahashi; Sirinupong, Nualpun; Alashi, Adeola M.; Aluko, Rotimi E.; Youravong, Wirote

doi:10.1016/j.jff.2018.07.041

Cited by 81 publications

(53 citation statements)

References 52 publications

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“…The total permeate (MBPH) obtained after 10 h of continuous hydrolysis coupled with membrane separation was collected, freeze-dried, and stored at −20 °C. The iron-binding capability of this product was determined using the method of Lee and Song [ 23 ] as previously modified [ 24 ]. Briefly, 5 mL MBPH (1 mg/mL) was mixed with 5 mL of 10 mM FeCl 2 ·4H 2 O prepared in 20 mM phosphate buffer, pH 7.0.…”

Section: Methodsmentioning

confidence: 99%

“…Values in the same column with different letters are significantly ( p < 0.05) different. 1 Data reported by Budseekoad et al [ 24 ]. HRSA, hydroxyl radical scavenging activity; SRSA, superoxide radical scavenging activity.…”

Section: Figurementioning

confidence: 99%

“…cEMR also has advantages over batch-type process, i.e., the minimal use of energy and enzymes. Mung bean is considered a good source of edible protein because of its high protein content, high bioavailability, and variety of amino acids [ 24 , 25 , 26 ]. The ACE-inhibitory and antioxidant activities of mung bean protein hydrolysates have been studied [ 24 , 27 ].…”

Section: Introductionmentioning

confidence: 99%

“…Mung bean is considered a good source of edible protein because of its high protein content, high bioavailability, and variety of amino acids [ 24 , 25 , 26 ]. The ACE-inhibitory and antioxidant activities of mung bean protein hydrolysates have been studied [ 24 , 27 ]. However, to the best of our knowledge, there is little information concerning the iron-binding bioactive peptides produced from mung bean protein hydrolysates using cEMR as well as their amino acid profile and sequences.…”

Section: Introductionmentioning

confidence: 99%

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

Chunkao

Youravong

Yupanqui

et al. 2020

Foods

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An iron-binding mung bean protein hydrolysate (MBPH) was prepared using a continuous enzymatic membrane reactor followed by peptide separation on anion-exchange (AEC) and reverse-phase HPLC (RP-HPLC) columns. Amino acid sequences of peptides present in the RP-HPLC fraction with the strongest iron-binding capacity were identified using mass spectrometry, and ten peptides of 5–8 amino acids synthesized for antioxidant characterization. Five fractions (AF1– AF5) with higher iron-binding capacity (88.86 ± 6.43 to 153.59 ± 2.18 mg/g peptide) when compared to the MBPH (36.81 ± 0.93 mg/g peptide) were obtained from AEC. PAIDL had the significantly (p < 0.05) highest iron-binding capacity, but LLLLG and LLGIL showed the strongest metal chelating activity. However, PAIDL (46.63%) and LLGIL (81.27%) had significantly (p < 0.05) better DPPH radical scavenging activity than the other peptides. PAIDL and LLGIL were also the most effective (p < 0.05) hydroxyl radical neutralizers with an effective concentration that scavenged 50% (EC50) values of 0.09 and 0.37 mM, respectively. PAIDL and AIVIL showed the lowest EC50 values of 0.07 mM each for superoxide radical scavenging activity. We conclude that short chain length in combination with leucine as the C-terminal amino acid residue contributed to the strong antioxidant properties of peptides in this study.

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Section: Methodsmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Chunkao

Youravong

Yupanqui

et al. 2020

Foods

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“…In recent years, many plants and animal iron-binding peptides have been purified. For example, iron-binding peptides from Pacific cod skin gelatin (Wu et al, 2017), fish scales collagen (Huang, Wu, Yang, Li, & Ku, 2015), porcine blood (Lee & Song, 2009), soybean protein (Lv et al, 2009), mung bean protein (Budseekoad et al, 2018), whey protein (Caetano-Silva, Bertoldo-Pacheco, Paes-Leme, & Netto, 2015;Cruz-Huerta et al, 2016), and others have been purified.…”

Section: Introductionmentioning

confidence: 99%

Purification of an iron‐binding peptide from scad ( Decapterus maruadsi ) processing by‐products and its effects on iron absorption by Caco‐2 cells

et al. 2019

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This work was aimed at producing peptides containing iron‐binding capabilities from scad (Decapterus maruadsi) processing by‐product with alcalase hydrolysis. The chelating peptides were purified by ultrafiltration, immobilized‐metal affinity chromatography, gel filtration chromatography, and reversed‐phase high‐performance liquid chromatography. A novel iron‐binding peptide was purified with 1,386.63 Da molecular weight and amino acid sequence of QKGTYDDYVEGL. The peptide binds to iron mainly through carboxyl and hydroxyl oxygen bonds. The iron‐binding peptide can significantly promote the absorption of inorganic iron in Caco‐2 cells. These results have contributed to development of the peptide from scad processing by‐products hydrolyzate in iron supplementations. Practical applications Iron deficiency is one of the most common and widespread nutritional disorders in the world. Iron‐peptide chelates may be suitable for iron‐fortification. Our study shows that a peptide purified from scad processing by‐product has iron‐chelating activity, and significantly increases iron absorption by Caco‐2 cells. Hence, this peptide has potential application as a novel carrier for enhancing iron absorption.

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Novel peptides with calcium‐binding capacity from antler bone hydrolysate, its bioactivity on MC3T3‐E1 cells, and the possible chelating mode

Wang,

Zhai,

Xiao

et al. 2024

Food Science & Nutrition

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In this study, peptide‐calcium chelate was screened from antler bone hydrolysate, and its bioactivity on MC3T3‐E1 cells and its chelating mechanism were investigated. In vitro experiments showed that peptide‐calcium chelate promoted the differentiation and mineralization of MC3T3‐E1 cells. Subsequently, three novel calcium‐chelating peptides were obtained from antler bone hydrolysate using hydroxyapatite chromatography (HAC), Sephadex G‐25 gel filtration chromatography, and reversed‐phase high‐performance liquid chromatography (RP‐HPLC). Meanwhile, this work determined peptides' amino acid sequences as TKLGTQLQL, LETVILGLLKT, and KMVFLMDLLK based on LC–MS/MS. Then the present work prepared the three peptides, with the corresponding calcium‐chelating rates being verified as 87.68 ± 2.86%, 80.72 ± 0.93%, and 67.96 ± 0.98%, respectively. Fourier transform infrared (FTIR) spectroscopy, ultraviolet–visible absorption (UV–vis) spectroscopy, X‐ray diffraction (XRD), circular dichroism (CD), zeta potential, and molecular dynamics (MD) simulations were adopted to investigate the chelating mode of peptides with calcium ions. As a result, oxygen in the carboxyl group and the nitrogen in the amino group were related to calcium binding. In addition, the chelation site preferred the negatively charged carboxylate groups of Leu or Thr. The present work revealed that antler bone might be the new calcium‐chelating peptide source and elucidated their positive role in osteogenesis.

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Structural and functional characterization of calcium and iron-binding peptides from mung bean protein hydrolysate

Cited by 81 publications

References 52 publications

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

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

Purification of an iron‐binding peptide from scad ( Decapterus maruadsi ) processing by‐products and its effects on iron absorption by Caco‐2 cells

Novel peptides with calcium‐binding capacity from antler bone hydrolysate, its bioactivity on MC3T3‐E1 cells, and the possible chelating mode

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