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 |
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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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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.</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 & 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. This study provides a theoretical basis for the development of new calcium supplement products that are absorbed easily. © 2024 Society of Chemical Industry.</description><subject>Absorption</subject><subject>Amino acid sequence</subject><subject>Amino acids</subject><subject>Amino groups</subject><subject>Bioavailability</subject><subject>Calcium</subject><subject>Calcium absorption</subject><subject>calcium binding ability</subject><subject>Calcium ions</subject><subject>Chelates</subject><subject>Chelation</subject><subject>Fourier analysis</subject><subject>Fourier transforms</subject><subject>Hydrolysates</subject><subject>identification</subject><subject>Industrial development</subject><subject>Infrared analysis</subject><subject>Legumes</subject><subject>Liquid chromatography</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Metal ions</subject><subject>Nucleotide sequence</subject><subject>peanut peptide</subject><subject>Peanuts</subject><subject>Peptides</subject><subject>promoting calcium absorption</subject><subject>Proteins</subject><subject>Scanning electron microscopy</subject><subject>separation</subject><subject>structural characteristics</subject><issn>0022-5142</issn><issn>1097-0010</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNp9kcFu1DAQhi0EotvCpQ-ALPWCkFI8tpOsj1VFaVElDsA5cpxx61USB9sBcoNn4A37JPV2lx56wJfxjD99Gusn5BjYKTDG32-i1acgpBLPyAqYqgvGgD0nq_zIixIkPyCHMW4YY0pV1UtyINalLJWUK_LnqsMxOeuMTs6P1FtqdG_cPFBzi30ejjd0wim5DiO1wQ-50-Oc6BR8QjfS26ULvl-iTkj12FHdRh-mB5k2yf1wadla9467338f_X6Yevz1irywuo_4el-PyLeLD1_PL4vrzx-vzs-uCyOgEkXZCQ3c8HzyhzqsSytUWSNqjtBabTRvOYAQiismVV3pfK9ra9cWZGVacUTe7rx58e8zxtQMLhrsez2in2MjGEjG1qAgoydP0I2fw5i3y1StKiXWkmXq3Y4ywccY0DZTcIMOSwOs2QbTbINpHoLJ8Ju9cm4H7B7Rf0lkAHbAT9fj8h9V8-nLxdlOeg9KKZtO</recordid><startdate>20240830</startdate><enddate>20240830</enddate><creator>Bu, Guanhao</creator><creator>Zhao, Xiaoling</creator><creator>Wang, Mengli</creator><creator>Ti, Guanghui</creator><creator>Chen, Fusheng</creator><creator>Duan, Xiaojie</creator><creator>Huang, Yanan</creator><creator>Li, Panxin</creator><general>John Wiley & Sons, Ltd</general><general>John Wiley and Sons, Limited</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QL</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-8201-1234</orcidid><orcidid>https://orcid.org/0000-0001-5867-986X</orcidid></search><sort><creationdate>20240830</creationdate><title>Identification of calcium chelating peptides from peanut protein hydrolysate and absorption activity of peptide–calcium complex</title><author>Bu, Guanhao ; Zhao, Xiaoling ; Wang, Mengli ; Ti, Guanghui ; Chen, Fusheng ; Duan, Xiaojie ; Huang, Yanan ; Li, Panxin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3163-5d3a12c2222142de75f3957eea2e1bfaca2b2113392904976a13377ff8f146cb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Absorption</topic><topic>Amino acid sequence</topic><topic>Amino acids</topic><topic>Amino groups</topic><topic>Bioavailability</topic><topic>Calcium</topic><topic>Calcium absorption</topic><topic>calcium binding ability</topic><topic>Calcium ions</topic><topic>Chelates</topic><topic>Chelation</topic><topic>Fourier analysis</topic><topic>Fourier transforms</topic><topic>Hydrolysates</topic><topic>identification</topic><topic>Industrial development</topic><topic>Infrared analysis</topic><topic>Legumes</topic><topic>Liquid chromatography</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Metal ions</topic><topic>Nucleotide sequence</topic><topic>peanut peptide</topic><topic>Peanuts</topic><topic>Peptides</topic><topic>promoting calcium absorption</topic><topic>Proteins</topic><topic>Scanning electron microscopy</topic><topic>separation</topic><topic>structural characteristics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><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><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the science of food and agriculture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bu, Guanhao</au><au>Zhao, Xiaoling</au><au>Wang, Mengli</au><au>Ti, Guanghui</au><au>Chen, Fusheng</au><au>Duan, Xiaojie</au><au>Huang, Yanan</au><au>Li, Panxin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of calcium chelating peptides from peanut protein hydrolysate and absorption activity of peptide–calcium complex</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J Sci Food Agric</addtitle><date>2024-08-30</date><risdate>2024</risdate><volume>104</volume><issue>11</issue><spage>6676</spage><epage>6686</epage><pages>6676-6686</pages><issn>0022-5142</issn><issn>1097-0010</issn><eissn>1097-0010</eissn><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.</abstract><cop>Chichester, UK</cop><pub>John Wiley & 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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