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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Veröffentlicht in:Journal of the science of food and agriculture 2024-08, Vol.104 (11), p.6676-6686
Hauptverfasser: Bu, Guanhao, Zhao, Xiaoling, Wang, Mengli, Ti, Guanghui, Chen, Fusheng, Duan, Xiaojie, Huang, Yanan, Li, Panxin
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container_end_page 6686
container_issue 11
container_start_page 6676
container_title Journal of the science of food and agriculture
container_volume 104
creator Bu, Guanhao
Zhao, Xiaoling
Wang, Mengli
Ti, Guanghui
Chen, Fusheng
Duan, Xiaojie
Huang, Yanan
Li, Panxin
description 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.
doi_str_mv 10.1002/jsfa.13493
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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.</description><identifier>ISSN: 0022-5142</identifier><identifier>ISSN: 1097-0010</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.13493</identifier><identifier>PMID: 38545944</identifier><language>eng</language><publisher>Chichester, UK: John Wiley &amp; Sons, Ltd</publisher><subject>Absorption ; Amino acid sequence ; Amino acids ; Amino groups ; Bioavailability ; Calcium ; Calcium absorption ; calcium binding ability ; Calcium ions ; Chelates ; Chelation ; Fourier analysis ; Fourier transforms ; Hydrolysates ; identification ; Industrial development ; Infrared analysis ; Legumes ; Liquid chromatography ; Mass spectrometry ; Mass spectroscopy ; Metal ions ; Nucleotide sequence ; peanut peptide ; Peanuts ; Peptides ; promoting calcium absorption ; Proteins ; Scanning electron microscopy ; separation ; structural characteristics</subject><ispartof>Journal of the science of food and agriculture, 2024-08, Vol.104 (11), p.6676-6686</ispartof><rights>2024 Society of Chemical Industry.</rights><rights>2024 Society of Chemical Industry</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3163-5d3a12c2222142de75f3957eea2e1bfaca2b2113392904976a13377ff8f146cb3</cites><orcidid>0000-0002-8201-1234 ; 0000-0001-5867-986X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjsfa.13493$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.13493$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38545944$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bu, Guanhao</creatorcontrib><creatorcontrib>Zhao, Xiaoling</creatorcontrib><creatorcontrib>Wang, Mengli</creatorcontrib><creatorcontrib>Ti, Guanghui</creatorcontrib><creatorcontrib>Chen, Fusheng</creatorcontrib><creatorcontrib>Duan, Xiaojie</creatorcontrib><creatorcontrib>Huang, Yanan</creatorcontrib><creatorcontrib>Li, Panxin</creatorcontrib><title>Identification of calcium chelating peptides from peanut protein hydrolysate and absorption activity of peptide–calcium complex</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>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. 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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.</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><pmid>38545944</pmid><doi>10.1002/jsfa.13493</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-8201-1234</orcidid><orcidid>https://orcid.org/0000-0001-5867-986X</orcidid></addata></record>
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subjects Absorption
Amino acid sequence
Amino acids
Amino groups
Bioavailability
Calcium
Calcium absorption
calcium binding ability
Calcium ions
Chelates
Chelation
Fourier analysis
Fourier transforms
Hydrolysates
identification
Industrial development
Infrared analysis
Legumes
Liquid chromatography
Mass spectrometry
Mass spectroscopy
Metal ions
Nucleotide sequence
peanut peptide
Peanuts
Peptides
promoting calcium absorption
Proteins
Scanning electron microscopy
separation
structural characteristics
title Identification of calcium chelating peptides from peanut protein hydrolysate and absorption activity of peptide–calcium complex
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