Study on preparation of acylated soy protein and stability of emulsion
BACKGROUND Protein can be used as an emulsifier to improve emulsion stability at the interface of water‐in‐oil emulsion. However, natural soybean protein isolate (SPI) does not meet the high demands as an emulsifier in the food industry. The effect of acylation modification by ethylenediaminetetraac...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2021-09, Vol.101 (12), p.4959-4968 |
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| container_title | Journal of the science of food and agriculture |
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| creator | Xia, Nan Lu, Xing‐Xing Zheng, Zhi Mu, Dong‐Dong Zhong, Xi‐Yang Luo, Shui‐Zhong Zhao, Yan‐Yan |
| description | BACKGROUND
Protein can be used as an emulsifier to improve emulsion stability at the interface of water‐in‐oil emulsion. However, natural soybean protein isolate (SPI) does not meet the high demands as an emulsifier in the food industry. The effect of acylation modification by ethylenediaminetetraacetic dianhydride (EDTAD; 0–300 g kg−1) on the physicochemical properties of SPI was studied.
RESULTS
The results of the Fourier transform infrared spectra analyses showed that carboxyl groups were introduced into the SPI structure by the EDTAD treatment. The carboxyl concentration of SPI was increased by 30–74.07% with an increase in EDTAD addition from 50 to 300 g kg−1. When 150 g kg−1 EDTAD was added, the surface hydrophobicity, the emulsifying activity, and the absolute value of the zeta potential were increased by 213%, 120%, and 68% respectively, and the particle size decreased to 247 nm. The droplet size of emulsion decreased to 10 μm when pH was 6. At the same concentration of SPI and pH, the absolute value of zeta potential of the emulsion was biggest. A comparison of the emulsions during storage showed the improvement of emulsion stability was related to the increase in the zeta potential and the decrease in the average particle size. The experimental group showed no destabilization on day 21, and no obvious aggregation phenomenon was observed.
CONCLUSION
Acylation modification by EDTAD changed the emulsifying properties of SPI and enhanced the stability of the SPI emulsion. © 2021 Society of Chemical Industry |
| doi_str_mv | 10.1002/jsfa.11139 |
| format | Article |
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Protein can be used as an emulsifier to improve emulsion stability at the interface of water‐in‐oil emulsion. However, natural soybean protein isolate (SPI) does not meet the high demands as an emulsifier in the food industry. The effect of acylation modification by ethylenediaminetetraacetic dianhydride (EDTAD; 0–300 g kg−1) on the physicochemical properties of SPI was studied.
RESULTS
The results of the Fourier transform infrared spectra analyses showed that carboxyl groups were introduced into the SPI structure by the EDTAD treatment. The carboxyl concentration of SPI was increased by 30–74.07% with an increase in EDTAD addition from 50 to 300 g kg−1. When 150 g kg−1 EDTAD was added, the surface hydrophobicity, the emulsifying activity, and the absolute value of the zeta potential were increased by 213%, 120%, and 68% respectively, and the particle size decreased to 247 nm. The droplet size of emulsion decreased to 10 μm when pH was 6. At the same concentration of SPI and pH, the absolute value of zeta potential of the emulsion was biggest. A comparison of the emulsions during storage showed the improvement of emulsion stability was related to the increase in the zeta potential and the decrease in the average particle size. The experimental group showed no destabilization on day 21, and no obvious aggregation phenomenon was observed.
CONCLUSION
Acylation modification by EDTAD changed the emulsifying properties of SPI and enhanced the stability of the SPI emulsion. © 2021 Society of Chemical Industry</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.11139</identifier><identifier>PMID: 33543501</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Acylation ; acylation modification ; Destabilization ; Emulsifiers ; emulsion stability ; Emulsions ; Emulsions - chemistry ; ethylenediaminetetraacetic dianhydride (EDTAD) ; Food industry ; Fourier transforms ; Glycine max - chemistry ; Hydrophobic and Hydrophilic Interactions ; Hydrophobicity ; Infrared analysis ; Infrared spectra ; Interface stability ; Particle Size ; pH effects ; Physicochemical properties ; Protein Stability ; Proteins ; soybean protein isolate (SPI) ; Soybean Proteins - chemistry ; Soybeans ; Zeta potential</subject><ispartof>Journal of the science of food and agriculture, 2021-09, Vol.101 (12), p.4959-4968</ispartof><rights>2021 Society of Chemical Industry</rights><rights>2021 Society of Chemical Industry.</rights><rights>Copyright © 2021 Society of Chemical Industry</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3579-9c4add833b09b30d8c2b090a898756a620238a8be2b0f52b624c2672881828453</citedby><cites>FETCH-LOGICAL-c3579-9c4add833b09b30d8c2b090a898756a620238a8be2b0f52b624c2672881828453</cites><orcidid>0000-0003-4138-0575 ; 0000-0003-4665-9735 ; 0000-0003-4879-2732</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.11139$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.11139$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33543501$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xia, Nan</creatorcontrib><creatorcontrib>Lu, Xing‐Xing</creatorcontrib><creatorcontrib>Zheng, Zhi</creatorcontrib><creatorcontrib>Mu, Dong‐Dong</creatorcontrib><creatorcontrib>Zhong, Xi‐Yang</creatorcontrib><creatorcontrib>Luo, Shui‐Zhong</creatorcontrib><creatorcontrib>Zhao, Yan‐Yan</creatorcontrib><title>Study on preparation of acylated soy protein and stability of emulsion</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>BACKGROUND
Protein can be used as an emulsifier to improve emulsion stability at the interface of water‐in‐oil emulsion. However, natural soybean protein isolate (SPI) does not meet the high demands as an emulsifier in the food industry. The effect of acylation modification by ethylenediaminetetraacetic dianhydride (EDTAD; 0–300 g kg−1) on the physicochemical properties of SPI was studied.
RESULTS
The results of the Fourier transform infrared spectra analyses showed that carboxyl groups were introduced into the SPI structure by the EDTAD treatment. The carboxyl concentration of SPI was increased by 30–74.07% with an increase in EDTAD addition from 50 to 300 g kg−1. When 150 g kg−1 EDTAD was added, the surface hydrophobicity, the emulsifying activity, and the absolute value of the zeta potential were increased by 213%, 120%, and 68% respectively, and the particle size decreased to 247 nm. The droplet size of emulsion decreased to 10 μm when pH was 6. At the same concentration of SPI and pH, the absolute value of zeta potential of the emulsion was biggest. A comparison of the emulsions during storage showed the improvement of emulsion stability was related to the increase in the zeta potential and the decrease in the average particle size. The experimental group showed no destabilization on day 21, and no obvious aggregation phenomenon was observed.
CONCLUSION
Acylation modification by EDTAD changed the emulsifying properties of SPI and enhanced the stability of the SPI emulsion. © 2021 Society of Chemical Industry</description><subject>Acylation</subject><subject>acylation modification</subject><subject>Destabilization</subject><subject>Emulsifiers</subject><subject>emulsion stability</subject><subject>Emulsions</subject><subject>Emulsions - chemistry</subject><subject>ethylenediaminetetraacetic dianhydride (EDTAD)</subject><subject>Food industry</subject><subject>Fourier transforms</subject><subject>Glycine max - chemistry</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobicity</subject><subject>Infrared analysis</subject><subject>Infrared spectra</subject><subject>Interface stability</subject><subject>Particle Size</subject><subject>pH effects</subject><subject>Physicochemical properties</subject><subject>Protein Stability</subject><subject>Proteins</subject><subject>soybean protein isolate (SPI)</subject><subject>Soybean Proteins - chemistry</subject><subject>Soybeans</subject><subject>Zeta potential</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMotlYv_gBZ8CLC1kmy2U2OpVg_KHionkM2m4WU_ajJLrL_vqlbPXjwNO_MPPMyvAhdY5hjAPKw9aWaY4ypOEFTDCKLATCcomlYkpjhhEzQhfdbABAiTc_RhFKWUAZ4ilabri-GqG2inTM75VRng27LSOmhUp0pIt8OYdd2xjaRakLfqdxWthsOlKn7yoeLS3RWqsqbq2OdoY_V4_vyOV6_Pb0sF-tYU5aJWOhEFQWnNAeRUyi4JkGB4oJnLFUpAUK54rkJ45KRPCWJJmlGOMec8ITRGbobfcNHn73xnayt16aqVGPa3kuS8Awz4CkE9PYPum1714TvJGGMQ8IJpoG6HyntWu-dKeXO2Vq5QWKQh3TlIV35nW6Ab46WfV6b4hf9iTMAeAS-bGWGf6zk62a1GE332_OCSA</recordid><startdate>202109</startdate><enddate>202109</enddate><creator>Xia, Nan</creator><creator>Lu, Xing‐Xing</creator><creator>Zheng, Zhi</creator><creator>Mu, Dong‐Dong</creator><creator>Zhong, Xi‐Yang</creator><creator>Luo, Shui‐Zhong</creator><creator>Zhao, Yan‐Yan</creator><general>John Wiley & Sons, Ltd</general><general>John Wiley and Sons, Limited</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>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/0000-0003-4138-0575</orcidid><orcidid>https://orcid.org/0000-0003-4665-9735</orcidid><orcidid>https://orcid.org/0000-0003-4879-2732</orcidid></search><sort><creationdate>202109</creationdate><title>Study on preparation of acylated soy protein and stability of emulsion</title><author>Xia, Nan ; Lu, Xing‐Xing ; Zheng, Zhi ; Mu, Dong‐Dong ; Zhong, Xi‐Yang ; Luo, Shui‐Zhong ; Zhao, Yan‐Yan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3579-9c4add833b09b30d8c2b090a898756a620238a8be2b0f52b624c2672881828453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Acylation</topic><topic>acylation modification</topic><topic>Destabilization</topic><topic>Emulsifiers</topic><topic>emulsion stability</topic><topic>Emulsions</topic><topic>Emulsions - chemistry</topic><topic>ethylenediaminetetraacetic dianhydride (EDTAD)</topic><topic>Food industry</topic><topic>Fourier transforms</topic><topic>Glycine max - chemistry</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Hydrophobicity</topic><topic>Infrared analysis</topic><topic>Infrared spectra</topic><topic>Interface stability</topic><topic>Particle Size</topic><topic>pH effects</topic><topic>Physicochemical properties</topic><topic>Protein Stability</topic><topic>Proteins</topic><topic>soybean protein isolate (SPI)</topic><topic>Soybean Proteins - chemistry</topic><topic>Soybeans</topic><topic>Zeta potential</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xia, Nan</creatorcontrib><creatorcontrib>Lu, Xing‐Xing</creatorcontrib><creatorcontrib>Zheng, Zhi</creatorcontrib><creatorcontrib>Mu, Dong‐Dong</creatorcontrib><creatorcontrib>Zhong, Xi‐Yang</creatorcontrib><creatorcontrib>Luo, Shui‐Zhong</creatorcontrib><creatorcontrib>Zhao, Yan‐Yan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><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>Xia, Nan</au><au>Lu, Xing‐Xing</au><au>Zheng, Zhi</au><au>Mu, Dong‐Dong</au><au>Zhong, Xi‐Yang</au><au>Luo, Shui‐Zhong</au><au>Zhao, Yan‐Yan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Study on preparation of acylated soy protein and stability of emulsion</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J Sci Food Agric</addtitle><date>2021-09</date><risdate>2021</risdate><volume>101</volume><issue>12</issue><spage>4959</spage><epage>4968</epage><pages>4959-4968</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><abstract>BACKGROUND
Protein can be used as an emulsifier to improve emulsion stability at the interface of water‐in‐oil emulsion. However, natural soybean protein isolate (SPI) does not meet the high demands as an emulsifier in the food industry. The effect of acylation modification by ethylenediaminetetraacetic dianhydride (EDTAD; 0–300 g kg−1) on the physicochemical properties of SPI was studied.
RESULTS
The results of the Fourier transform infrared spectra analyses showed that carboxyl groups were introduced into the SPI structure by the EDTAD treatment. The carboxyl concentration of SPI was increased by 30–74.07% with an increase in EDTAD addition from 50 to 300 g kg−1. When 150 g kg−1 EDTAD was added, the surface hydrophobicity, the emulsifying activity, and the absolute value of the zeta potential were increased by 213%, 120%, and 68% respectively, and the particle size decreased to 247 nm. The droplet size of emulsion decreased to 10 μm when pH was 6. At the same concentration of SPI and pH, the absolute value of zeta potential of the emulsion was biggest. A comparison of the emulsions during storage showed the improvement of emulsion stability was related to the increase in the zeta potential and the decrease in the average particle size. The experimental group showed no destabilization on day 21, and no obvious aggregation phenomenon was observed.
CONCLUSION
Acylation modification by EDTAD changed the emulsifying properties of SPI and enhanced the stability of the SPI emulsion. © 2021 Society of Chemical Industry</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>33543501</pmid><doi>10.1002/jsfa.11139</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-4138-0575</orcidid><orcidid>https://orcid.org/0000-0003-4665-9735</orcidid><orcidid>https://orcid.org/0000-0003-4879-2732</orcidid></addata></record> |
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| subjects | Acylation acylation modification Destabilization Emulsifiers emulsion stability Emulsions Emulsions - chemistry ethylenediaminetetraacetic dianhydride (EDTAD) Food industry Fourier transforms Glycine max - chemistry Hydrophobic and Hydrophilic Interactions Hydrophobicity Infrared analysis Infrared spectra Interface stability Particle Size pH effects Physicochemical properties Protein Stability Proteins soybean protein isolate (SPI) Soybean Proteins - chemistry Soybeans Zeta potential |
| title | Study on preparation of acylated soy protein and stability of emulsion |
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