Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides
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-bi...
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MDPI AG
2020-10-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/9/10/1406 |
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| author | Siriporn Chunkao Wirote Youravong Chutha T. Yupanqui Adeola M. Alashi Rotimi E. Aluko |
| author_facet | Siriporn Chunkao Wirote Youravong Chutha T. Yupanqui Adeola M. Alashi Rotimi E. Aluko |
| author_sort | Siriporn Chunkao |
| collection | DOAJ |
| description | 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 (<i>p</i> < 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 (<i>p</i> < 0.05) better DPPH radical scavenging activity than the other peptides. PAIDL and LLGIL were also the most effective (<i>p</i> < 0.05) hydroxyl radical neutralizers with an effective concentration that scavenged 50% (EC<sub>50</sub>) values of 0.09 and 0.37 mM, respectively. PAIDL and AIVIL showed the lowest EC<sub>50</sub> values of 0.07 mM each for superoxide radical scavenging activity. We conclude that short chain length in combination with leucine as the <i>C</i>-terminal amino acid residue contributed to the strong antioxidant properties of peptides in this study. |
| first_indexed | 2024-03-10T15:52:07Z |
| format | Article |
| id | doaj.art-cbf43af646d3499fb88177fdbb616fe9 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T15:52:07Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-cbf43af646d3499fb88177fdbb616fe92023-11-20T15:59:36ZengMDPI AGFoods2304-81582020-10-01910140610.3390/foods9101406Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant PeptidesSiriporn Chunkao0Wirote Youravong1Chutha T. Yupanqui2Adeola M. Alashi3Rotimi E. Aluko4Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90110, ThailandDepartment of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90110, ThailandCentre of Excellence in Functional Foods and Nutraceuticals, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90110, ThailandDepartment of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, MB R3T 2N2, CanadaDepartment of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, MB R3T 2N2, CanadaAn 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 (<i>p</i> < 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 (<i>p</i> < 0.05) better DPPH radical scavenging activity than the other peptides. PAIDL and LLGIL were also the most effective (<i>p</i> < 0.05) hydroxyl radical neutralizers with an effective concentration that scavenged 50% (EC<sub>50</sub>) values of 0.09 and 0.37 mM, respectively. PAIDL and AIVIL showed the lowest EC<sub>50</sub> values of 0.07 mM each for superoxide radical scavenging activity. We conclude that short chain length in combination with leucine as the <i>C</i>-terminal amino acid residue contributed to the strong antioxidant properties of peptides in this study.https://www.mdpi.com/2304-8158/9/10/1406mung beanironpancreatinpeptidescontinuous enzymatic membrane reactorantioxidant |
| spellingShingle | Siriporn Chunkao Wirote Youravong Chutha T. Yupanqui Adeola M. Alashi Rotimi E. Aluko Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides Foods mung bean iron pancreatin peptides continuous enzymatic membrane reactor antioxidant |
| title | Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides |
| title_full | Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides |
| title_fullStr | Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides |
| title_full_unstemmed | Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides |
| title_short | Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides |
| title_sort | structure and function of mung bean protein derived iron binding antioxidant peptides |
| topic | mung bean iron pancreatin peptides continuous enzymatic membrane reactor antioxidant |
| url | https://www.mdpi.com/2304-8158/9/10/1406 |
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