Interaction between pea protein isolate and quercetin: Effects on protein conformation and quercetin activity
Comprehensive comprehension of the interaction between proteins and polyphenols is crucial for advancing their utilization in food processing. This study investigated no‐covalent interaction between pea protein isolate (PPI) and quercetin (Que) through spectroscopic analysis and molecular simulation...
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| Veröffentlicht in: | Journal of food science 2024-11, Vol.89 (11), p.7549-7560 |
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| creator | Huang, Siyun Zhou, Haili Lin, Jiaxin Yin, Xin Xiong, Tao Peng, Fei |
| description | Comprehensive comprehension of the interaction between proteins and polyphenols is crucial for advancing their utilization in food processing. This study investigated no‐covalent interaction between pea protein isolate (PPI) and quercetin (Que) through spectroscopic analysis and molecular simulation. Fourier transform infrared spectroscopy and circular dichroism spectrum showed that the interaction between PPI and Que changed the secondary structure of the protein due to a decrease in α‐helix content and an increase in the random coil. Thermodynamic parameters indicated that the Quebound PPI via hydrogen bonds and hydrophobic interactions (ΔH > 0, ΔS > 0, and ΔG |
| doi_str_mv | 10.1111/1750-3841.17384 |
| format | Article |
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Practical Application
Interaction between pea protein isolate and quercetin can change the protein conformation to maintain the stability of quercetin and is helpful to expand the market value and application value of plant protein. The research has important implications for using leguminous protein as embedded support to improve the stability of polyphenols compounds.</description><identifier>ISSN: 0022-1147</identifier><identifier>ISSN: 1750-3841</identifier><identifier>EISSN: 1750-3841</identifier><identifier>DOI: 10.1111/1750-3841.17384</identifier><identifier>PMID: 39349982</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Antioxidants - chemistry ; Antioxidants - pharmacology ; binding mechanism ; Bioavailability ; Chemical bonds ; Circular Dichroism ; Dichroism ; Food plants ; Food processing ; Fourier analysis ; Fourier transforms ; Functional foods & nutraceuticals ; Hydrogen Bonding ; Hydrogen bonds ; Hydrophobic and Hydrophilic Interactions ; Hydrophobicity ; Infrared analysis ; Infrared spectroscopy ; Market value ; Molecular docking ; Molecular Docking Simulation ; Molecular structure ; multispectral technique ; noncovalent interaction ; Particle Size ; pea protein isolate ; Pea Proteins - chemistry ; Peas ; Pisum sativum - chemistry ; Polyphenols ; Polyphenols - chemistry ; Polyphenols - pharmacology ; Protein Conformation ; Protein structure ; Protein Structure, Secondary ; Proteins ; Quercetin ; Quercetin - chemistry ; Quercetin - pharmacology ; Random coil ; Secondary structure ; Spectroscopy, Fourier Transform Infrared - methods ; Stability ; Thermodynamics</subject><ispartof>Journal of food science, 2024-11, Vol.89 (11), p.7549-7560</ispartof><rights>2024 Institute of Food Technologists.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c2564-20eabca22551f62998034f956d4eb36cc1d1d127d0646f009cc686ef3280fca93</cites><orcidid>0000-0002-7486-734X ; 0000-0001-5370-8676</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2F1750-3841.17384$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2F1750-3841.17384$$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/39349982$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Huang, Siyun</creatorcontrib><creatorcontrib>Zhou, Haili</creatorcontrib><creatorcontrib>Lin, Jiaxin</creatorcontrib><creatorcontrib>Yin, Xin</creatorcontrib><creatorcontrib>Xiong, Tao</creatorcontrib><creatorcontrib>Peng, Fei</creatorcontrib><title>Interaction between pea protein isolate and quercetin: Effects on protein conformation and quercetin activity</title><title>Journal of food science</title><addtitle>J Food Sci</addtitle><description>Comprehensive comprehension of the interaction between proteins and polyphenols is crucial for advancing their utilization in food processing. This study investigated no‐covalent interaction between pea protein isolate (PPI) and quercetin (Que) through spectroscopic analysis and molecular simulation. Fourier transform infrared spectroscopy and circular dichroism spectrum showed that the interaction between PPI and Que changed the secondary structure of the protein due to a decrease in α‐helix content and an increase in the random coil. Thermodynamic parameters indicated that the Quebound PPI via hydrogen bonds and hydrophobic interactions (ΔH > 0, ΔS > 0, and ΔG < 0), which was also confirmed by molecular docking. Particle size and ζ‐potential showed that PPI and Que demonstrated effective interaction and binding capabilities, enhancing the stability. In addition, the antioxidant and bioaccessibility of complexes have also been enhanced. This study shed a light on the application of protein–polyphenol complexes for developing functional foods.
Practical Application
Interaction between pea protein isolate and quercetin can change the protein conformation to maintain the stability of quercetin and is helpful to expand the market value and application value of plant protein. The research has important implications for using leguminous protein as embedded support to improve the stability of polyphenols compounds.</description><subject>Antioxidants - chemistry</subject><subject>Antioxidants - pharmacology</subject><subject>binding mechanism</subject><subject>Bioavailability</subject><subject>Chemical bonds</subject><subject>Circular Dichroism</subject><subject>Dichroism</subject><subject>Food plants</subject><subject>Food processing</subject><subject>Fourier analysis</subject><subject>Fourier transforms</subject><subject>Functional foods & nutraceuticals</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobicity</subject><subject>Infrared analysis</subject><subject>Infrared spectroscopy</subject><subject>Market value</subject><subject>Molecular docking</subject><subject>Molecular Docking Simulation</subject><subject>Molecular structure</subject><subject>multispectral technique</subject><subject>noncovalent interaction</subject><subject>Particle Size</subject><subject>pea protein isolate</subject><subject>Pea Proteins - chemistry</subject><subject>Peas</subject><subject>Pisum sativum - chemistry</subject><subject>Polyphenols</subject><subject>Polyphenols - chemistry</subject><subject>Polyphenols - pharmacology</subject><subject>Protein Conformation</subject><subject>Protein structure</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Quercetin</subject><subject>Quercetin - chemistry</subject><subject>Quercetin - pharmacology</subject><subject>Random coil</subject><subject>Secondary structure</subject><subject>Spectroscopy, Fourier Transform Infrared - methods</subject><subject>Stability</subject><subject>Thermodynamics</subject><issn>0022-1147</issn><issn>1750-3841</issn><issn>1750-3841</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1LxDAQxYMoun6cvUnAi5fu5qNNW2-yuroieFDPIU0nUGnTNcm67H9valXQizOHIeE3j8cbhE4pmdJYM5pnJOFFSqc0j2MHTX5-dtGEEMYSStP8AB16_0qGNxf76ICXPC3Lgk1Qt7QBnNKh6S2uIGwALF6BwivXB2gsbnzfqgBY2Rq_rcFpCI29xDfGgA4ex61vUvfW9K5Tn1K_cDzovzdhe4z2jGo9nHzNI_SyuHme3yUPj7fL-dVDolkm0oQRUJVWjGUZNYJFp4SnpsxEnULFhda0js3ymohUGEJKrUUhwHBWEKNVyY_QxagbvUUXPsiu8RraVlno117ymJ3guRBpRM__oK_92tnoLlJMlIQWlEdqNlLa9d47MHLlmk65raREDpeQQ-5yyF1-XiJunH3prqsO6h_-O_oIiBHYNC1s_9OT94vrp1H5Azp4k3E</recordid><startdate>202411</startdate><enddate>202411</enddate><creator>Huang, Siyun</creator><creator>Zhou, Haili</creator><creator>Lin, Jiaxin</creator><creator>Yin, Xin</creator><creator>Xiong, Tao</creator><creator>Peng, Fei</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QR</scope><scope>7ST</scope><scope>7T7</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-7486-734X</orcidid><orcidid>https://orcid.org/0000-0001-5370-8676</orcidid></search><sort><creationdate>202411</creationdate><title>Interaction between pea protein isolate and quercetin: Effects on protein conformation and quercetin activity</title><author>Huang, Siyun ; Zhou, Haili ; Lin, Jiaxin ; Yin, Xin ; Xiong, Tao ; Peng, Fei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2564-20eabca22551f62998034f956d4eb36cc1d1d127d0646f009cc686ef3280fca93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Antioxidants - chemistry</topic><topic>Antioxidants - pharmacology</topic><topic>binding mechanism</topic><topic>Bioavailability</topic><topic>Chemical bonds</topic><topic>Circular Dichroism</topic><topic>Dichroism</topic><topic>Food plants</topic><topic>Food processing</topic><topic>Fourier analysis</topic><topic>Fourier transforms</topic><topic>Functional foods & nutraceuticals</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Hydrophobicity</topic><topic>Infrared analysis</topic><topic>Infrared spectroscopy</topic><topic>Market value</topic><topic>Molecular docking</topic><topic>Molecular Docking Simulation</topic><topic>Molecular structure</topic><topic>multispectral technique</topic><topic>noncovalent interaction</topic><topic>Particle Size</topic><topic>pea protein isolate</topic><topic>Pea Proteins - chemistry</topic><topic>Peas</topic><topic>Pisum sativum - chemistry</topic><topic>Polyphenols</topic><topic>Polyphenols - chemistry</topic><topic>Polyphenols - pharmacology</topic><topic>Protein Conformation</topic><topic>Protein structure</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Quercetin</topic><topic>Quercetin - chemistry</topic><topic>Quercetin - pharmacology</topic><topic>Random coil</topic><topic>Secondary structure</topic><topic>Spectroscopy, Fourier Transform Infrared - methods</topic><topic>Stability</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huang, Siyun</creatorcontrib><creatorcontrib>Zhou, Haili</creatorcontrib><creatorcontrib>Lin, Jiaxin</creatorcontrib><creatorcontrib>Yin, Xin</creatorcontrib><creatorcontrib>Xiong, Tao</creatorcontrib><creatorcontrib>Peng, Fei</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Toxicology Abstracts</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>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of food science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, Siyun</au><au>Zhou, Haili</au><au>Lin, Jiaxin</au><au>Yin, Xin</au><au>Xiong, Tao</au><au>Peng, Fei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction between pea protein isolate and quercetin: Effects on protein conformation and quercetin activity</atitle><jtitle>Journal of food science</jtitle><addtitle>J Food Sci</addtitle><date>2024-11</date><risdate>2024</risdate><volume>89</volume><issue>11</issue><spage>7549</spage><epage>7560</epage><pages>7549-7560</pages><issn>0022-1147</issn><issn>1750-3841</issn><eissn>1750-3841</eissn><abstract>Comprehensive comprehension of the interaction between proteins and polyphenols is crucial for advancing their utilization in food processing. This study investigated no‐covalent interaction between pea protein isolate (PPI) and quercetin (Que) through spectroscopic analysis and molecular simulation. Fourier transform infrared spectroscopy and circular dichroism spectrum showed that the interaction between PPI and Que changed the secondary structure of the protein due to a decrease in α‐helix content and an increase in the random coil. Thermodynamic parameters indicated that the Quebound PPI via hydrogen bonds and hydrophobic interactions (ΔH > 0, ΔS > 0, and ΔG < 0), which was also confirmed by molecular docking. Particle size and ζ‐potential showed that PPI and Que demonstrated effective interaction and binding capabilities, enhancing the stability. In addition, the antioxidant and bioaccessibility of complexes have also been enhanced. This study shed a light on the application of protein–polyphenol complexes for developing functional foods.
Practical Application
Interaction between pea protein isolate and quercetin can change the protein conformation to maintain the stability of quercetin and is helpful to expand the market value and application value of plant protein. The research has important implications for using leguminous protein as embedded support to improve the stability of polyphenols compounds.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>39349982</pmid><doi>10.1111/1750-3841.17384</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-7486-734X</orcidid><orcidid>https://orcid.org/0000-0001-5370-8676</orcidid></addata></record> |
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| subjects | Antioxidants - chemistry Antioxidants - pharmacology binding mechanism Bioavailability Chemical bonds Circular Dichroism Dichroism Food plants Food processing Fourier analysis Fourier transforms Functional foods & nutraceuticals Hydrogen Bonding Hydrogen bonds Hydrophobic and Hydrophilic Interactions Hydrophobicity Infrared analysis Infrared spectroscopy Market value Molecular docking Molecular Docking Simulation Molecular structure multispectral technique noncovalent interaction Particle Size pea protein isolate Pea Proteins - chemistry Peas Pisum sativum - chemistry Polyphenols Polyphenols - chemistry Polyphenols - pharmacology Protein Conformation Protein structure Protein Structure, Secondary Proteins Quercetin Quercetin - chemistry Quercetin - pharmacology Random coil Secondary structure Spectroscopy, Fourier Transform Infrared - methods Stability Thermodynamics |
| title | Interaction between pea protein isolate and quercetin: Effects on protein conformation and quercetin activity |
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