Identification of calcium chelating peptides from peanut protein hydrolysate and absorption activity of peptide–calcium complex
BACKGROUND Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide–calcium complex. RESULTS Peptides with high calcium chelating rate were isolated and purified from pe...
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| Vydáno v: | Journal of the science of food and agriculture Ročník 104; číslo 11; s. 6676 - 6686 |
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| Hlavní autoři: | , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
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Chichester, UK
John Wiley & Sons, Ltd
30.08.2024
John Wiley and Sons, Limited |
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| ISSN: | 0022-5142, 1097-0010, 1097-0010 |
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| Abstract | BACKGROUND
Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide–calcium complex.
RESULTS
Peptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography–tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide–calcium complex (PPH21‐Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco‐2 cell model tests revealed that the bioavailability of PPH21‐Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%.
CONCLUSION
Peanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide–calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry. |
|---|---|
| AbstractList | BACKGROUND: Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide–calcium complex. RESULTS: Peptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography–tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide–calcium complex (PPH21‐Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco‐2 cell model tests revealed that the bioavailability of PPH21‐Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%. CONCLUSION: Peanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide–calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry. BACKGROUNDPeanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide–calcium complex.RESULTSPeptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography–tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide–calcium complex (PPH21‐Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco‐2 cell model tests revealed that the bioavailability of PPH21‐Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%.CONCLUSIONPeanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide–calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry. Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide-calcium complex.BACKGROUNDPeanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide-calcium complex.Peptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography-tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide-calcium complex (PPH21-Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco-2 cell model tests revealed that the bioavailability of PPH21-Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%.RESULTSPeptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography-tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide-calcium complex (PPH21-Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco-2 cell model tests revealed that the bioavailability of PPH21-Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%.Peanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide-calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry.CONCLUSIONPeanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide-calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry. BACKGROUND Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide–calcium complex. RESULTS Peptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography–tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide–calcium complex (PPH21‐Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco‐2 cell model tests revealed that the bioavailability of PPH21‐Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%. CONCLUSION Peanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide–calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry. Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and absorption properties of peptide-calcium complex. Peptides with high calcium chelating rate were isolated and purified from peanut protein hydrolysate (PPH), and the chelation rate of component F21 was higher (81.4 ± 0.8%). Six peptides were identified from component F21 by liquid chromatography-tandem mass spectrometry, and the frequency of acidic amino acids and arginine in the amino acid sequence was higher in all six peptides. Peanut peptide-calcium complex (PPH21-Ca) was prepared by selecting component F21 (PPH21). Ultraviolet analysis indicated that the chelate reaction occurred between peanut peptide and calcium ions. Fourier transform infrared analysis showed that the chelating sites were carboxyl and amino groups on the amino acid residues of peptides. Scanning electron microscopy revealed that the surface of peanut peptide had a smooth block structure, but the surface of the complex had a granular morphology. Caco-2 cell model tests revealed that the bioavailability of PPH21-Ca was 58.4 ± 0.5%, which was significantly higher than that of inorganic calcium at 37.0 ± 0.4%. Peanut peptides can chelate calcium ions by carboxyl and amino groups, and the peptide-calcium complex had higher bioavailability. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry. |
| Author | Chen, Fusheng Huang, Yanan Zhao, Xiaoling Wang, Mengli Li, Panxin Duan, Xiaojie Bu, Guanhao Ti, Guanghui |
| Author_xml | – sequence: 1 givenname: Guanhao orcidid: 0000-0001-5867-986X surname: Bu fullname: Bu, Guanhao email: buguanhao2008@126.com organization: Henan University of Technology – sequence: 2 givenname: Xiaoling surname: Zhao fullname: Zhao, Xiaoling organization: Henan University of Technology – sequence: 3 givenname: Mengli surname: Wang fullname: Wang, Mengli organization: Henan University of Technology – sequence: 4 givenname: Guanghui surname: Ti fullname: Ti, Guanghui organization: Henan University of Technology – sequence: 5 givenname: Fusheng orcidid: 0000-0002-8201-1234 surname: Chen fullname: Chen, Fusheng organization: Henan University of Technology – sequence: 6 givenname: Xiaojie surname: Duan fullname: Duan, Xiaojie organization: Henan University of Technology – sequence: 7 givenname: Yanan surname: Huang fullname: Huang, Yanan organization: Henan Province Nanjie Village (Group) Co., Ltd – sequence: 8 givenname: Panxin surname: Li fullname: Li, Panxin organization: Henan Province Nanjie Village (Group) Co., Ltd |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/38545944$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1016_j_foodres_2025_117160 crossref_primary_10_1016_j_ijbiomac_2024_138404 crossref_primary_10_1021_acs_jafc_5c09028 crossref_primary_10_3390_foods14091594 crossref_primary_10_1016_j_foodres_2025_117128 crossref_primary_10_3390_w17121757 crossref_primary_10_1039_D4FO04403G crossref_primary_10_1016_j_bcab_2025_103770 crossref_primary_10_1016_j_ijbiomac_2025_147326 crossref_primary_10_1016_j_jff_2025_106953 crossref_primary_10_1016_j_fbio_2025_107030 |
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| Keywords | peanut peptide promoting calcium absorption calcium binding ability identification separation structural characteristics |
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Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with... Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with calcium and... BACKGROUNDPeanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with... BACKGROUND: Peanut peptides have good chelating ability with metal ions. However, there are few studies on the chelation mechanism of peanut peptides with... |
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| SubjectTerms | Absorption agriculture Amino acid sequence amino acid sequences Amino acids Amino groups arginine Bioavailability Calcium Calcium absorption calcium binding ability Calcium ions Chelates Chelation electron microscopy Fourier analysis Fourier transform infrared spectroscopy Fourier transforms human cell lines Hydrolysates identification Industrial development Infrared analysis Legumes Liquid chromatography Mass spectrometry Mass spectroscopy Metal ions Nucleotide sequence peanut peptide peanut protein Peanuts Peptides promoting calcium absorption protein hydrolysates Proteins Scanning electron microscopy separation structural characteristics tandem mass spectrometry |
| Title | Identification of calcium chelating peptides from peanut protein hydrolysate and absorption activity of peptide–calcium complex |
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