Formation of whey protein, pectin, and chlorogenic acid ternary complexes and their application in emulsions
Physicochemical properties, stability, and digestive behavior of lycopene-loaded emulsions prepared by ternary complexes fabricated with different mixing sequences based on whey protein isolate (WPI), high methoxyl pectin (HMP), and chlorogenic acid (CA) were investigated. Spectroscopic and molecula...
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Veröffentlicht in: | International journal of biological macromolecules 2024-12, Vol.283 (Pt 3), p.137871, Article 137871 |
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creator | Zhang, Yuanyuan Lu, Yingcong Liu, Yaxuan Zhao, Ru Huang, Xin Wang, Cuina Zhang, Tiehua |
description | Physicochemical properties, stability, and digestive behavior of lycopene-loaded emulsions prepared by ternary complexes fabricated with different mixing sequences based on whey protein isolate (WPI), high methoxyl pectin (HMP), and chlorogenic acid (CA) were investigated. Spectroscopic and molecular docking analyses confirmed the non-covalent interactions among the compounds within the ternary complexes, as well as the conformational changes in the protein induced by the mixing sequence. The interfacial tension (6.92–9.44 mN/m) influenced by the different mixing sequences of WPI, HMP and CA was HMP-CA-WPI > WPI-CA-HMP > WPI-HMP-CA, and the size of emulsions stabilized by HMP-CA-WPI was approximately 10 nm larger than that of the other two. Complexes with mixing sequence of HMP, CA and WPI outperformed in antioxidant properties (Ferric reducing power absorbance 0.43, ABTS∙ radical scavenging activity 66.04 %), lycopene retention rate (after UV irradiation 85.11 %, after thermal treatment 83.15 %), and storage stability of emulsions than those prepared by WPI-HMP-CA and WPI-CA-HMP. Emulsions stabilized by different ternary complexes showed similar free fatty acid release profiles (39.62 %–41.59 %) and lycopene bio-accessibility (28.87 %–29.94 %) during digestion. This study mat offer novel insights for the rational utilization in emulsions of ternary complexes based on proteins, polysaccharides, and phenolic acids.
•Lycopene-loaded emulsions stabilized by WPI, HMP, and CA were examined with different mixing sequences.•Spectroscopic and molecular docking analysis confirmed non-covalent interactions and WPI conformational changes.•The HMP-CA-WPI sequence showed superior antioxidant properties, lycopene retention, and stability.•Different mixing sequences emulsions had similar FFA release and lycopene bio-accessibility during digestion. |
doi_str_mv | 10.1016/j.ijbiomac.2024.137871 |
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•Lycopene-loaded emulsions stabilized by WPI, HMP, and CA were examined with different mixing sequences.•Spectroscopic and molecular docking analysis confirmed non-covalent interactions and WPI conformational changes.•The HMP-CA-WPI sequence showed superior antioxidant properties, lycopene retention, and stability.•Different mixing sequences emulsions had similar FFA release and lycopene bio-accessibility during digestion.</description><identifier>ISSN: 0141-8130</identifier><identifier>ISSN: 1879-0003</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2024.137871</identifier><identifier>PMID: 39566761</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Antioxidants - chemistry ; Chlorogenic acid ; Chlorogenic Acid - chemistry ; Emulsion ; Emulsions - chemistry ; Lycopene ; Lycopene - chemistry ; Mixing sequence ; Molecular Docking Simulation ; Pectin ; Pectins - chemistry ; Whey protein ; Whey Proteins - chemistry</subject><ispartof>International journal of biological macromolecules, 2024-12, Vol.283 (Pt 3), p.137871, Article 137871</ispartof><rights>2024 Elsevier B.V.</rights><rights>Copyright © 2024 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c245t-4ddd725969fca05f09fe4d6ed587b90fe11f09d7294e6af41494e2d1c99123593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2024.137871$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39566761$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Yuanyuan</creatorcontrib><creatorcontrib>Lu, Yingcong</creatorcontrib><creatorcontrib>Liu, Yaxuan</creatorcontrib><creatorcontrib>Zhao, Ru</creatorcontrib><creatorcontrib>Huang, Xin</creatorcontrib><creatorcontrib>Wang, Cuina</creatorcontrib><creatorcontrib>Zhang, Tiehua</creatorcontrib><title>Formation of whey protein, pectin, and chlorogenic acid ternary complexes and their application in emulsions</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>Physicochemical properties, stability, and digestive behavior of lycopene-loaded emulsions prepared by ternary complexes fabricated with different mixing sequences based on whey protein isolate (WPI), high methoxyl pectin (HMP), and chlorogenic acid (CA) were investigated. Spectroscopic and molecular docking analyses confirmed the non-covalent interactions among the compounds within the ternary complexes, as well as the conformational changes in the protein induced by the mixing sequence. The interfacial tension (6.92–9.44 mN/m) influenced by the different mixing sequences of WPI, HMP and CA was HMP-CA-WPI > WPI-CA-HMP > WPI-HMP-CA, and the size of emulsions stabilized by HMP-CA-WPI was approximately 10 nm larger than that of the other two. Complexes with mixing sequence of HMP, CA and WPI outperformed in antioxidant properties (Ferric reducing power absorbance 0.43, ABTS∙ radical scavenging activity 66.04 %), lycopene retention rate (after UV irradiation 85.11 %, after thermal treatment 83.15 %), and storage stability of emulsions than those prepared by WPI-HMP-CA and WPI-CA-HMP. Emulsions stabilized by different ternary complexes showed similar free fatty acid release profiles (39.62 %–41.59 %) and lycopene bio-accessibility (28.87 %–29.94 %) during digestion. This study mat offer novel insights for the rational utilization in emulsions of ternary complexes based on proteins, polysaccharides, and phenolic acids.
•Lycopene-loaded emulsions stabilized by WPI, HMP, and CA were examined with different mixing sequences.•Spectroscopic and molecular docking analysis confirmed non-covalent interactions and WPI conformational changes.•The HMP-CA-WPI sequence showed superior antioxidant properties, lycopene retention, and stability.•Different mixing sequences emulsions had similar FFA release and lycopene bio-accessibility during digestion.</description><subject>Antioxidants - chemistry</subject><subject>Chlorogenic acid</subject><subject>Chlorogenic Acid - chemistry</subject><subject>Emulsion</subject><subject>Emulsions - chemistry</subject><subject>Lycopene</subject><subject>Lycopene - chemistry</subject><subject>Mixing sequence</subject><subject>Molecular Docking Simulation</subject><subject>Pectin</subject><subject>Pectins - chemistry</subject><subject>Whey protein</subject><subject>Whey Proteins - chemistry</subject><issn>0141-8130</issn><issn>1879-0003</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PwzAMhiMEgvHxF1COHOiImzZtbiDEAAmJC5yjLHFZprYpScfHvyejwJWTLeuxrfch5BTYHBiIi_XcrZfOd9rMc5YXc-BVXcEOmUFdyYwxxnfJjEEBWQ2cHZDDGNdpKkqo98kBl6UQlYAZaRc-dHp0vqe-oe8r_KRD8CO6_pwOaMZt1b2lZtX64F-wd4Zq4ywdMfQ6fFLju6HFD4zf2LhCF6gehtaZ6arrKXabNqY-HpO9RrcRT37qEXle3Dxd32UPj7f311cPmcmLcswKa22Vl1LIxmhWNkw2WFiBtqyrpWQNAqRZQmSBQjcFFKnJLRgpIeel5EfkbLqborxuMI6qc9Fg2-oe_SYqDjztJDE8oWJCTfAxBmzUEFyXgilgamtardWvabU1rSbTafH058dm2aH9W_tVm4DLCcCU9M1hUNE47A1aF5JYZb3778cXO6CT9A</recordid><startdate>20241201</startdate><enddate>20241201</enddate><creator>Zhang, Yuanyuan</creator><creator>Lu, Yingcong</creator><creator>Liu, Yaxuan</creator><creator>Zhao, Ru</creator><creator>Huang, Xin</creator><creator>Wang, Cuina</creator><creator>Zhang, Tiehua</creator><general>Elsevier B.V</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>7X8</scope></search><sort><creationdate>20241201</creationdate><title>Formation of whey protein, pectin, and chlorogenic acid ternary complexes and their application in emulsions</title><author>Zhang, Yuanyuan ; Lu, Yingcong ; Liu, Yaxuan ; Zhao, Ru ; Huang, Xin ; Wang, Cuina ; Zhang, Tiehua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c245t-4ddd725969fca05f09fe4d6ed587b90fe11f09d7294e6af41494e2d1c99123593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Antioxidants - chemistry</topic><topic>Chlorogenic acid</topic><topic>Chlorogenic Acid - chemistry</topic><topic>Emulsion</topic><topic>Emulsions - chemistry</topic><topic>Lycopene</topic><topic>Lycopene - chemistry</topic><topic>Mixing sequence</topic><topic>Molecular Docking Simulation</topic><topic>Pectin</topic><topic>Pectins - chemistry</topic><topic>Whey protein</topic><topic>Whey Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Yuanyuan</creatorcontrib><creatorcontrib>Lu, Yingcong</creatorcontrib><creatorcontrib>Liu, Yaxuan</creatorcontrib><creatorcontrib>Zhao, Ru</creatorcontrib><creatorcontrib>Huang, Xin</creatorcontrib><creatorcontrib>Wang, Cuina</creatorcontrib><creatorcontrib>Zhang, Tiehua</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Yuanyuan</au><au>Lu, Yingcong</au><au>Liu, Yaxuan</au><au>Zhao, Ru</au><au>Huang, Xin</au><au>Wang, Cuina</au><au>Zhang, Tiehua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Formation of whey protein, pectin, and chlorogenic acid ternary complexes and their application in emulsions</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2024-12-01</date><risdate>2024</risdate><volume>283</volume><issue>Pt 3</issue><spage>137871</spage><pages>137871-</pages><artnum>137871</artnum><issn>0141-8130</issn><issn>1879-0003</issn><eissn>1879-0003</eissn><abstract>Physicochemical properties, stability, and digestive behavior of lycopene-loaded emulsions prepared by ternary complexes fabricated with different mixing sequences based on whey protein isolate (WPI), high methoxyl pectin (HMP), and chlorogenic acid (CA) were investigated. Spectroscopic and molecular docking analyses confirmed the non-covalent interactions among the compounds within the ternary complexes, as well as the conformational changes in the protein induced by the mixing sequence. The interfacial tension (6.92–9.44 mN/m) influenced by the different mixing sequences of WPI, HMP and CA was HMP-CA-WPI > WPI-CA-HMP > WPI-HMP-CA, and the size of emulsions stabilized by HMP-CA-WPI was approximately 10 nm larger than that of the other two. Complexes with mixing sequence of HMP, CA and WPI outperformed in antioxidant properties (Ferric reducing power absorbance 0.43, ABTS∙ radical scavenging activity 66.04 %), lycopene retention rate (after UV irradiation 85.11 %, after thermal treatment 83.15 %), and storage stability of emulsions than those prepared by WPI-HMP-CA and WPI-CA-HMP. Emulsions stabilized by different ternary complexes showed similar free fatty acid release profiles (39.62 %–41.59 %) and lycopene bio-accessibility (28.87 %–29.94 %) during digestion. This study mat offer novel insights for the rational utilization in emulsions of ternary complexes based on proteins, polysaccharides, and phenolic acids.
•Lycopene-loaded emulsions stabilized by WPI, HMP, and CA were examined with different mixing sequences.•Spectroscopic and molecular docking analysis confirmed non-covalent interactions and WPI conformational changes.•The HMP-CA-WPI sequence showed superior antioxidant properties, lycopene retention, and stability.•Different mixing sequences emulsions had similar FFA release and lycopene bio-accessibility during digestion.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>39566761</pmid><doi>10.1016/j.ijbiomac.2024.137871</doi></addata></record> |
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subjects | Antioxidants - chemistry Chlorogenic acid Chlorogenic Acid - chemistry Emulsion Emulsions - chemistry Lycopene Lycopene - chemistry Mixing sequence Molecular Docking Simulation Pectin Pectins - chemistry Whey protein Whey Proteins - chemistry |
title | Formation of whey protein, pectin, and chlorogenic acid ternary complexes and their application in emulsions |
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