The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength
BACKGROUND To clarify the role of the extension region on the structure–functional relationship of the α‐subunit of β‐conglycinin, α‐subunit and its segment of the core region (αc‐subunit) were expressed via an Escherichia coli system. Their physicochemical properties were compared under acid, neutr...
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| Veröffentlicht in: | Journal of the science of food and agriculture 2022-10, Vol.102 (13), p.6062-6070 |
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| creator | Yuan, Yanqiu He, Zijie Ju, Qian Zhao, Sibo Wu, Chang Hu, Yayun Zhou, Shuyi Luan, Guangzhong |
| description | BACKGROUND
To clarify the role of the extension region on the structure–functional relationship of the α‐subunit of β‐conglycinin, α‐subunit and its segment of the core region (αc‐subunit) were expressed via an Escherichia coli system. Their physicochemical properties were compared under acid, neutral or alkaline conditions (pH 4.0, 7.0, and 8.0) and high or low ionic strength (μ = 0.05 and 0.5), respectively.
RESULTS
The results showed that the extension region contributed to increasing thermal stability, especially at low ionic strength under acidic and neutral conditions. The extension region stabilized the α‐subunit with high solubility, low turbidity, and small particle size under neutral and alkaline conditions, whereas these impacts were suppressed at a high ionic strength and acidic conditions. Surface hydrophobicity of the α‐subunit decreased under acidic and alkaline conditions without being interfered with by ionic strength.
CONCLUSION
It can be concluded that the extension region played different roles under different pH and ionic strength conditions. These factors should be specified carefully and speculated individually to explore the more detailed and profound nature of β‐conglycinin at the submolecular level. The results could benefit a better understanding of the relationship between domain structure and functions of soybean protein. © 2022 Society of Chemical Industry. |
| doi_str_mv | 10.1002/jsfa.11958 |
| format | Article |
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To clarify the role of the extension region on the structure–functional relationship of the α‐subunit of β‐conglycinin, α‐subunit and its segment of the core region (αc‐subunit) were expressed via an Escherichia coli system. Their physicochemical properties were compared under acid, neutral or alkaline conditions (pH 4.0, 7.0, and 8.0) and high or low ionic strength (μ = 0.05 and 0.5), respectively.
RESULTS
The results showed that the extension region contributed to increasing thermal stability, especially at low ionic strength under acidic and neutral conditions. The extension region stabilized the α‐subunit with high solubility, low turbidity, and small particle size under neutral and alkaline conditions, whereas these impacts were suppressed at a high ionic strength and acidic conditions. Surface hydrophobicity of the α‐subunit decreased under acidic and alkaline conditions without being interfered with by ionic strength.
CONCLUSION
It can be concluded that the extension region played different roles under different pH and ionic strength conditions. These factors should be specified carefully and speculated individually to explore the more detailed and profound nature of β‐conglycinin at the submolecular level. The results could benefit a better understanding of the relationship between domain structure and functions of soybean protein. © 2022 Society of Chemical Industry.</description><identifier>ISSN: 0022-5142</identifier><identifier>EISSN: 1097-0010</identifier><identifier>DOI: 10.1002/jsfa.11958</identifier><identifier>PMID: 35462432</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Antigens, Plant - chemistry ; Conglycinin ; E coli ; extension region ; Globulins - chemistry ; Glycine max - chemistry ; Hydrogen-Ion Concentration ; Hydrophobicity ; Ionic strength ; Osmolar Concentration ; pH effects ; Physicochemical properties ; recombinant protein ; Seed Storage Proteins - chemistry ; soybean protein ; Soybean Proteins - chemistry ; Soybeans ; structure–function relationship ; subunit ; Thermal stability ; Turbidity ; β‐conglycinin</subject><ispartof>Journal of the science of food and agriculture, 2022-10, Vol.102 (13), p.6062-6070</ispartof><rights>2022 Society of Chemical Industry.</rights><rights>Copyright © 2022 Society of Chemical Industry</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3168-75ec1b616fdf1ac081b2e160c97432313f646654185d1d379096fabf6d5bc2bc3</cites><orcidid>0000-0003-0307-9888 ; 0000-0003-0287-0504</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.11958$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjsfa.11958$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35462432$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yuan, Yanqiu</creatorcontrib><creatorcontrib>He, Zijie</creatorcontrib><creatorcontrib>Ju, Qian</creatorcontrib><creatorcontrib>Zhao, Sibo</creatorcontrib><creatorcontrib>Wu, Chang</creatorcontrib><creatorcontrib>Hu, Yayun</creatorcontrib><creatorcontrib>Zhou, Shuyi</creatorcontrib><creatorcontrib>Luan, Guangzhong</creatorcontrib><title>The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength</title><title>Journal of the science of food and agriculture</title><addtitle>J Sci Food Agric</addtitle><description>BACKGROUND
To clarify the role of the extension region on the structure–functional relationship of the α‐subunit of β‐conglycinin, α‐subunit and its segment of the core region (αc‐subunit) were expressed via an Escherichia coli system. Their physicochemical properties were compared under acid, neutral or alkaline conditions (pH 4.0, 7.0, and 8.0) and high or low ionic strength (μ = 0.05 and 0.5), respectively.
RESULTS
The results showed that the extension region contributed to increasing thermal stability, especially at low ionic strength under acidic and neutral conditions. The extension region stabilized the α‐subunit with high solubility, low turbidity, and small particle size under neutral and alkaline conditions, whereas these impacts were suppressed at a high ionic strength and acidic conditions. Surface hydrophobicity of the α‐subunit decreased under acidic and alkaline conditions without being interfered with by ionic strength.
CONCLUSION
It can be concluded that the extension region played different roles under different pH and ionic strength conditions. These factors should be specified carefully and speculated individually to explore the more detailed and profound nature of β‐conglycinin at the submolecular level. The results could benefit a better understanding of the relationship between domain structure and functions of soybean protein. © 2022 Society of Chemical Industry.</description><subject>Antigens, Plant - chemistry</subject><subject>Conglycinin</subject><subject>E coli</subject><subject>extension region</subject><subject>Globulins - chemistry</subject><subject>Glycine max - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrophobicity</subject><subject>Ionic strength</subject><subject>Osmolar Concentration</subject><subject>pH effects</subject><subject>Physicochemical properties</subject><subject>recombinant protein</subject><subject>Seed Storage Proteins - chemistry</subject><subject>soybean protein</subject><subject>Soybean Proteins - chemistry</subject><subject>Soybeans</subject><subject>structure–function relationship</subject><subject>subunit</subject><subject>Thermal stability</subject><subject>Turbidity</subject><subject>β‐conglycinin</subject><issn>0022-5142</issn><issn>1097-0010</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU9u1DAUxi0EokNhwwFQJDYIKcXPTpwJu6qiFFSJBWUdOc7LxCPHCf5TmB1H4B6s4CA9BCfBmWlZsECy9OzPv_c9Wx8hT4GeAKXs1db38gSgLtf3yApoXeWUAr1PVumS5SUU7Ig88n5LKa1rIR6SI14WghWcrciPqwEzNxnMpj4LaY9fA1qvJ5s53CwlrUX3wUUVopMmk7bL5mHntZrUgKNWSVODdFIFdNoHrfyd283P39---9hGq8Oi3fxKZzXZjdkpbbV9nelxNskhpFH7rvkiu5Ym4n5KErVaRqPdhOExedBL4_HJbT0mn87fXJ1d5Jcf3r47O73MFQexzqsSFbQCRN_1IBVdQ8sQBFV1lb7MgfeiEKIsYF120PGqprXoZduLrmwVaxU_Ji8OvrObPkf0oRm1V2iMtDhF3zBRlkC54HVCn_-DbqfobHpdw6oUBas5qxL18kApN3nvsG9mp0fpdg3QZomwWSJs9hEm-NmtZWxH7P6id5klAA7AF21w9x-r5v3H89OD6R9ahKyD</recordid><startdate>202210</startdate><enddate>202210</enddate><creator>Yuan, Yanqiu</creator><creator>He, Zijie</creator><creator>Ju, Qian</creator><creator>Zhao, Sibo</creator><creator>Wu, Chang</creator><creator>Hu, Yayun</creator><creator>Zhou, Shuyi</creator><creator>Luan, Guangzhong</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/0000-0003-0307-9888</orcidid><orcidid>https://orcid.org/0000-0003-0287-0504</orcidid></search><sort><creationdate>202210</creationdate><title>The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength</title><author>Yuan, Yanqiu ; He, Zijie ; Ju, Qian ; Zhao, Sibo ; Wu, Chang ; Hu, Yayun ; Zhou, Shuyi ; Luan, Guangzhong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3168-75ec1b616fdf1ac081b2e160c97432313f646654185d1d379096fabf6d5bc2bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Antigens, Plant - chemistry</topic><topic>Conglycinin</topic><topic>E coli</topic><topic>extension region</topic><topic>Globulins - chemistry</topic><topic>Glycine max - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrophobicity</topic><topic>Ionic strength</topic><topic>Osmolar Concentration</topic><topic>pH effects</topic><topic>Physicochemical properties</topic><topic>recombinant protein</topic><topic>Seed Storage Proteins - chemistry</topic><topic>soybean protein</topic><topic>Soybean Proteins - chemistry</topic><topic>Soybeans</topic><topic>structure–function relationship</topic><topic>subunit</topic><topic>Thermal stability</topic><topic>Turbidity</topic><topic>β‐conglycinin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yuan, Yanqiu</creatorcontrib><creatorcontrib>He, Zijie</creatorcontrib><creatorcontrib>Ju, Qian</creatorcontrib><creatorcontrib>Zhao, Sibo</creatorcontrib><creatorcontrib>Wu, Chang</creatorcontrib><creatorcontrib>Hu, Yayun</creatorcontrib><creatorcontrib>Zhou, Shuyi</creatorcontrib><creatorcontrib>Luan, Guangzhong</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>Yuan, Yanqiu</au><au>He, Zijie</au><au>Ju, Qian</au><au>Zhao, Sibo</au><au>Wu, Chang</au><au>Hu, Yayun</au><au>Zhou, Shuyi</au><au>Luan, Guangzhong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength</atitle><jtitle>Journal of the science of food and agriculture</jtitle><addtitle>J Sci Food Agric</addtitle><date>2022-10</date><risdate>2022</risdate><volume>102</volume><issue>13</issue><spage>6062</spage><epage>6070</epage><pages>6062-6070</pages><issn>0022-5142</issn><eissn>1097-0010</eissn><abstract>BACKGROUND
To clarify the role of the extension region on the structure–functional relationship of the α‐subunit of β‐conglycinin, α‐subunit and its segment of the core region (αc‐subunit) were expressed via an Escherichia coli system. Their physicochemical properties were compared under acid, neutral or alkaline conditions (pH 4.0, 7.0, and 8.0) and high or low ionic strength (μ = 0.05 and 0.5), respectively.
RESULTS
The results showed that the extension region contributed to increasing thermal stability, especially at low ionic strength under acidic and neutral conditions. The extension region stabilized the α‐subunit with high solubility, low turbidity, and small particle size under neutral and alkaline conditions, whereas these impacts were suppressed at a high ionic strength and acidic conditions. Surface hydrophobicity of the α‐subunit decreased under acidic and alkaline conditions without being interfered with by ionic strength.
CONCLUSION
It can be concluded that the extension region played different roles under different pH and ionic strength conditions. These factors should be specified carefully and speculated individually to explore the more detailed and profound nature of β‐conglycinin at the submolecular level. The results could benefit a better understanding of the relationship between domain structure and functions of soybean protein. © 2022 Society of Chemical Industry.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>35462432</pmid><doi>10.1002/jsfa.11958</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-0307-9888</orcidid><orcidid>https://orcid.org/0000-0003-0287-0504</orcidid></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Antigens, Plant - chemistry Conglycinin E coli extension region Globulins - chemistry Glycine max - chemistry Hydrogen-Ion Concentration Hydrophobicity Ionic strength Osmolar Concentration pH effects Physicochemical properties recombinant protein Seed Storage Proteins - chemistry soybean protein Soybean Proteins - chemistry Soybeans structure–function relationship subunit Thermal stability Turbidity β‐conglycinin |
| title | The role of the extension region on the structural and physicochemical characteristics of the α‐subunit of β‐conglycinin: implications of pH value and ionic strength |
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