Effects of malondialdehyde‐induced protein oxidation on the structural characteristics of rice protein
Summary Malondialdehyde (MDA) was selected to represent a secondary by‐product of lipid peroxidation during rice ageing. This study aimed to investigate the effects of MDA modification on the structural characteristics of rice protein. The results showed that as MDA concentration increased, rice pro...
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| Veröffentlicht in: | International journal of food science & technology 2020-02, Vol.55 (2), p.760-768 |
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| creator | Li, Fang Wu, Xiao‐Juan Wu, Wei |
| description | Summary
Malondialdehyde (MDA) was selected to represent a secondary by‐product of lipid peroxidation during rice ageing. This study aimed to investigate the effects of MDA modification on the structural characteristics of rice protein. The results showed that as MDA concentration increased, rice protein carbonyl and disulphide groups increased, but sulphydryl content decreased. The blue shift of maximum fluorescence peak, the decrease of rice protein intrinsic fluorescence intensity and the reduction of surface hydrophobicity indicated the formation of protein aggregates caused by MDA oxidative modification. The results of molecular weight distribution and particle size distribution showed that MDA modification resulted in the formation of soluble protein aggregates, and the decrease of rice protein solubility indicated that insoluble protein aggregates were formed. Results of protein electrophoresis showed that MDA modification contributed to rice protein aggregation via non‐disulphide covalent bonds. The results showed that rice protein gradually aggregated with increasing MDA concentration.
MDA modification induce rice protein oxidation. |
| doi_str_mv | 10.1111/ijfs.14379 |
| format | Article |
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Malondialdehyde (MDA) was selected to represent a secondary by‐product of lipid peroxidation during rice ageing. This study aimed to investigate the effects of MDA modification on the structural characteristics of rice protein. The results showed that as MDA concentration increased, rice protein carbonyl and disulphide groups increased, but sulphydryl content decreased. The blue shift of maximum fluorescence peak, the decrease of rice protein intrinsic fluorescence intensity and the reduction of surface hydrophobicity indicated the formation of protein aggregates caused by MDA oxidative modification. The results of molecular weight distribution and particle size distribution showed that MDA modification resulted in the formation of soluble protein aggregates, and the decrease of rice protein solubility indicated that insoluble protein aggregates were formed. Results of protein electrophoresis showed that MDA modification contributed to rice protein aggregation via non‐disulphide covalent bonds. The results showed that rice protein gradually aggregated with increasing MDA concentration.
MDA modification induce rice protein oxidation.</description><identifier>ISSN: 0950-5423</identifier><identifier>EISSN: 1365-2621</identifier><identifier>DOI: 10.1111/ijfs.14379</identifier><language>eng</language><publisher>Oxford: Wiley Subscription Services, Inc</publisher><subject>Aggregates ; Aggregation ; Aging ; Carbonyl compounds ; Carbonyls ; Covalent bonds ; Disulfides ; Electrophoresis ; Fluorescence ; Hydrophobicity ; Lipid peroxidation ; Lipids ; Malondialdehyde ; Molecular weight ; Molecular weight distribution ; Oxidation ; Particle size distribution ; Peroxidation ; Protein interaction ; protein oxidation ; Proteins ; Rice ; rice ageing ; rice protein ; Size distribution</subject><ispartof>International journal of food science & technology, 2020-02, Vol.55 (2), p.760-768</ispartof><rights>2019 Institute of Food Science and Technology</rights><rights>International Journal of Food Science and Technology © 2020 Institute of Food Science and Technology</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3389-56b41c8c542c47ca093d02b5b436a1ceb96bd8895d6583731b9a0d21d9000c653</citedby><cites>FETCH-LOGICAL-c3389-56b41c8c542c47ca093d02b5b436a1ceb96bd8895d6583731b9a0d21d9000c653</cites><orcidid>0000-0002-5466-3139 ; 0000-0002-8966-0421 ; 0000-0001-9229-6360</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%2Fijfs.14379$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fijfs.14379$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids></links><search><creatorcontrib>Li, Fang</creatorcontrib><creatorcontrib>Wu, Xiao‐Juan</creatorcontrib><creatorcontrib>Wu, Wei</creatorcontrib><title>Effects of malondialdehyde‐induced protein oxidation on the structural characteristics of rice protein</title><title>International journal of food science & technology</title><description>Summary
Malondialdehyde (MDA) was selected to represent a secondary by‐product of lipid peroxidation during rice ageing. This study aimed to investigate the effects of MDA modification on the structural characteristics of rice protein. The results showed that as MDA concentration increased, rice protein carbonyl and disulphide groups increased, but sulphydryl content decreased. The blue shift of maximum fluorescence peak, the decrease of rice protein intrinsic fluorescence intensity and the reduction of surface hydrophobicity indicated the formation of protein aggregates caused by MDA oxidative modification. The results of molecular weight distribution and particle size distribution showed that MDA modification resulted in the formation of soluble protein aggregates, and the decrease of rice protein solubility indicated that insoluble protein aggregates were formed. Results of protein electrophoresis showed that MDA modification contributed to rice protein aggregation via non‐disulphide covalent bonds. The results showed that rice protein gradually aggregated with increasing MDA concentration.
MDA modification induce rice protein oxidation.</description><subject>Aggregates</subject><subject>Aggregation</subject><subject>Aging</subject><subject>Carbonyl compounds</subject><subject>Carbonyls</subject><subject>Covalent bonds</subject><subject>Disulfides</subject><subject>Electrophoresis</subject><subject>Fluorescence</subject><subject>Hydrophobicity</subject><subject>Lipid peroxidation</subject><subject>Lipids</subject><subject>Malondialdehyde</subject><subject>Molecular weight</subject><subject>Molecular weight distribution</subject><subject>Oxidation</subject><subject>Particle size distribution</subject><subject>Peroxidation</subject><subject>Protein interaction</subject><subject>protein oxidation</subject><subject>Proteins</subject><subject>Rice</subject><subject>rice ageing</subject><subject>rice protein</subject><subject>Size distribution</subject><issn>0950-5423</issn><issn>1365-2621</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp9kE1OwzAQhS0EEqWw4QSR2CGl-CdO4iWqChRVYgGsLWfsKK7SpNiOoDuOwBk5CW4DW2Yzs_jem5mH0CXBMxLrxq5rPyMZK8QRmhCW85TmlByjCRYcpzyj7BSdeb_GGFNWZBPULOraQPBJXycb1fadtqrVptlp8_35ZTs9gNHJ1vXB2C7pP6xWwfZx6pLQmMQHN0AYnGoTaJRTEIyzPlg4GDoL5k97jk5q1Xpz8dun6PVu8TJ_SFdP98v57SoFxkqR8rzKCJQQT4WsAIUF05hWvMpYrgiYSuSVLkvBdc5LVjBSCYU1JVrElyDnbIquRt-4920wPsh1P7gurpSUZZwSKgoWqeuRAtd770wtt85ulNtJguU-SblPUh6SjDAZ4Xfbmt0_pFw-3j2Pmh_htXhU</recordid><startdate>202002</startdate><enddate>202002</enddate><creator>Li, Fang</creator><creator>Wu, Xiao‐Juan</creator><creator>Wu, Wei</creator><general>Wiley Subscription Services, Inc</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>SOI</scope><orcidid>https://orcid.org/0000-0002-5466-3139</orcidid><orcidid>https://orcid.org/0000-0002-8966-0421</orcidid><orcidid>https://orcid.org/0000-0001-9229-6360</orcidid></search><sort><creationdate>202002</creationdate><title>Effects of malondialdehyde‐induced protein oxidation on the structural characteristics of rice protein</title><author>Li, Fang ; Wu, Xiao‐Juan ; Wu, Wei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3389-56b41c8c542c47ca093d02b5b436a1ceb96bd8895d6583731b9a0d21d9000c653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Aggregates</topic><topic>Aggregation</topic><topic>Aging</topic><topic>Carbonyl compounds</topic><topic>Carbonyls</topic><topic>Covalent bonds</topic><topic>Disulfides</topic><topic>Electrophoresis</topic><topic>Fluorescence</topic><topic>Hydrophobicity</topic><topic>Lipid peroxidation</topic><topic>Lipids</topic><topic>Malondialdehyde</topic><topic>Molecular weight</topic><topic>Molecular weight distribution</topic><topic>Oxidation</topic><topic>Particle size distribution</topic><topic>Peroxidation</topic><topic>Protein interaction</topic><topic>protein oxidation</topic><topic>Proteins</topic><topic>Rice</topic><topic>rice ageing</topic><topic>rice protein</topic><topic>Size distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Fang</creatorcontrib><creatorcontrib>Wu, Xiao‐Juan</creatorcontrib><creatorcontrib>Wu, Wei</creatorcontrib><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity 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>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>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><jtitle>International journal of food science & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Fang</au><au>Wu, Xiao‐Juan</au><au>Wu, Wei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of malondialdehyde‐induced protein oxidation on the structural characteristics of rice protein</atitle><jtitle>International journal of food science & technology</jtitle><date>2020-02</date><risdate>2020</risdate><volume>55</volume><issue>2</issue><spage>760</spage><epage>768</epage><pages>760-768</pages><issn>0950-5423</issn><eissn>1365-2621</eissn><abstract>Summary
Malondialdehyde (MDA) was selected to represent a secondary by‐product of lipid peroxidation during rice ageing. This study aimed to investigate the effects of MDA modification on the structural characteristics of rice protein. The results showed that as MDA concentration increased, rice protein carbonyl and disulphide groups increased, but sulphydryl content decreased. The blue shift of maximum fluorescence peak, the decrease of rice protein intrinsic fluorescence intensity and the reduction of surface hydrophobicity indicated the formation of protein aggregates caused by MDA oxidative modification. The results of molecular weight distribution and particle size distribution showed that MDA modification resulted in the formation of soluble protein aggregates, and the decrease of rice protein solubility indicated that insoluble protein aggregates were formed. Results of protein electrophoresis showed that MDA modification contributed to rice protein aggregation via non‐disulphide covalent bonds. The results showed that rice protein gradually aggregated with increasing MDA concentration.
MDA modification induce rice protein oxidation.</abstract><cop>Oxford</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1111/ijfs.14379</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-5466-3139</orcidid><orcidid>https://orcid.org/0000-0002-8966-0421</orcidid><orcidid>https://orcid.org/0000-0001-9229-6360</orcidid></addata></record> |
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| source | Oxford Journals Open Access Collection; Wiley Online Library Journals Frontfile Complete |
| subjects | Aggregates Aggregation Aging Carbonyl compounds Carbonyls Covalent bonds Disulfides Electrophoresis Fluorescence Hydrophobicity Lipid peroxidation Lipids Malondialdehyde Molecular weight Molecular weight distribution Oxidation Particle size distribution Peroxidation Protein interaction protein oxidation Proteins Rice rice ageing rice protein Size distribution |
| title | Effects of malondialdehyde‐induced protein oxidation on the structural characteristics of rice protein |
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