Effect of Enzymatic Deamidation on the Heat-induced Conformational Changes in Whey Protein Isolate and Its Relation to Gel Properties
The effect of protein-glutaminase (PG) on the heat-induced conformational changes in whey protein isolate (WPI) and its relation to gel properties was investigated. The structural properties of WPI treated with PG were examined by several analytical methods. The analysis of the fluorescence spectrum...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2013-03, Vol.61 (9), p.2205-2212 |
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| container_issue | 9 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Miwa, Noriko Yokoyama, Keiichi Nio, Noriki Sonomoto, Kenji |
| description | The effect of protein-glutaminase (PG) on the heat-induced conformational changes in whey protein isolate (WPI) and its relation to gel properties was investigated. The structural properties of WPI treated with PG were examined by several analytical methods. The analysis of the fluorescence spectrum and the binding capacity of a fluorescent probe demonstrated that deamidation prevented the increase in the fluorescence intensity caused by subsequent heat treatment. Measurements of the molecular weight distribution of WPI showed that PG-treated WPI was not likely to polymerize even after heating. This is thought to be due to an increase in electrostatic repulsion between carboxylic acid groups and a decrease in the formation of disulfide bonds, which results in the decrease in heat-induced aggregation. The properties of heat-induced WPI gels were modified by deamidation. PG-treated WPI gels had a soft texture and a high water-holding capacity in the presence of salts. |
| doi_str_mv | 10.1021/jf3047626 |
| format | Article |
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The structural properties of WPI treated with PG were examined by several analytical methods. The analysis of the fluorescence spectrum and the binding capacity of a fluorescent probe demonstrated that deamidation prevented the increase in the fluorescence intensity caused by subsequent heat treatment. Measurements of the molecular weight distribution of WPI showed that PG-treated WPI was not likely to polymerize even after heating. This is thought to be due to an increase in electrostatic repulsion between carboxylic acid groups and a decrease in the formation of disulfide bonds, which results in the decrease in heat-induced aggregation. The properties of heat-induced WPI gels were modified by deamidation. PG-treated WPI gels had a soft texture and a high water-holding capacity in the presence of salts.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf3047626</identifier><identifier>PMID: 23379844</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Ammonia - metabolism ; analytical methods ; binding capacity ; Biological and medical sciences ; deamidation ; disulfide bonds ; electrostatic interactions ; fluorescence ; Fluorescent Dyes ; Food industries ; Fundamental and applied biological sciences. Psychology ; gels ; Gels - chemistry ; Glutaminase - metabolism ; heat treatment ; Hot Temperature ; Milk and cheese industries. Ice creams ; Milk Proteins - chemistry ; Milk Proteins - metabolism ; Molecular Weight ; polymerization ; Protein Conformation ; salts ; Spectrometry, Fluorescence ; texture ; water holding capacity ; whey protein isolate ; Whey Proteins</subject><ispartof>Journal of agricultural and food chemistry, 2013-03, Vol.61 (9), p.2205-2212</ispartof><rights>Copyright © 2013 American Chemical Society</rights><rights>2014 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a435t-5546e4f19ff79d5634d6ebc1f033faaf25cf96043e27471338fc2d2f20578fb33</citedby><cites>FETCH-LOGICAL-a435t-5546e4f19ff79d5634d6ebc1f033faaf25cf96043e27471338fc2d2f20578fb33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf3047626$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf3047626$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=27193613$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23379844$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miwa, Noriko</creatorcontrib><creatorcontrib>Yokoyama, Keiichi</creatorcontrib><creatorcontrib>Nio, Noriki</creatorcontrib><creatorcontrib>Sonomoto, Kenji</creatorcontrib><title>Effect of Enzymatic Deamidation on the Heat-induced Conformational Changes in Whey Protein Isolate and Its Relation to Gel Properties</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The effect of protein-glutaminase (PG) on the heat-induced conformational changes in whey protein isolate (WPI) and its relation to gel properties was investigated. The structural properties of WPI treated with PG were examined by several analytical methods. The analysis of the fluorescence spectrum and the binding capacity of a fluorescent probe demonstrated that deamidation prevented the increase in the fluorescence intensity caused by subsequent heat treatment. Measurements of the molecular weight distribution of WPI showed that PG-treated WPI was not likely to polymerize even after heating. This is thought to be due to an increase in electrostatic repulsion between carboxylic acid groups and a decrease in the formation of disulfide bonds, which results in the decrease in heat-induced aggregation. The properties of heat-induced WPI gels were modified by deamidation. PG-treated WPI gels had a soft texture and a high water-holding capacity in the presence of salts.</description><subject>Ammonia - metabolism</subject><subject>analytical methods</subject><subject>binding capacity</subject><subject>Biological and medical sciences</subject><subject>deamidation</subject><subject>disulfide bonds</subject><subject>electrostatic interactions</subject><subject>fluorescence</subject><subject>Fluorescent Dyes</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gels</subject><subject>Gels - chemistry</subject><subject>Glutaminase - metabolism</subject><subject>heat treatment</subject><subject>Hot Temperature</subject><subject>Milk and cheese industries. Ice creams</subject><subject>Milk Proteins - chemistry</subject><subject>Milk Proteins - metabolism</subject><subject>Molecular Weight</subject><subject>polymerization</subject><subject>Protein Conformation</subject><subject>salts</subject><subject>Spectrometry, Fluorescence</subject><subject>texture</subject><subject>water holding capacity</subject><subject>whey protein isolate</subject><subject>Whey Proteins</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0ctuEzEUBmALgWgoLHgB8AapXUzxdS5LFEIbqVIRULEcnXjOaSaaGae2ZxH2fW8mJG03SJZsy59-Hf1m7L0UF1Io-XlDWpgiV_kLNpNWicxKWb5kMzE9ZqXN5Ql7E-NGCFHaQrxmJ0rroiqNmbGHBRG6xD3xxfBn10NqHf-K0LfNdPQDn1ZaI79CSFk7NKPDhs_9QD70_wB0fL6G4Q4jbwf-e407_j34hNNlGX0HCTkMDV-myH9gd8hMnl9it3dbDKnF-Ja9Iugivjvup-z22-LX_Cq7vrlczr9cZ2C0TZm1JkdDsiIqqsbm2jQ5rpwkoTUBkLKOqlwYjaowhdS6JKcaRUrYoqSV1qfs7JC7Df5-xJjqvo0Ouw4G9GOspcmVLAtTyomeH6gLPsaAVG9D20PY1VLU-9brp9Yn--EYO656bJ7kY80T-HQEEB10FGBwbXx2hax0LvfzfTw4Al_DXZjM7U8lpBFCKlFp8ZwELtYbP4bpA-J_RvoLHVeelA</recordid><startdate>20130306</startdate><enddate>20130306</enddate><creator>Miwa, Noriko</creator><creator>Yokoyama, Keiichi</creator><creator>Nio, Noriki</creator><creator>Sonomoto, Kenji</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>IQODW</scope><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>20130306</creationdate><title>Effect of Enzymatic Deamidation on the Heat-induced Conformational Changes in Whey Protein Isolate and Its Relation to Gel Properties</title><author>Miwa, Noriko ; Yokoyama, Keiichi ; Nio, Noriki ; Sonomoto, Kenji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a435t-5546e4f19ff79d5634d6ebc1f033faaf25cf96043e27471338fc2d2f20578fb33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Ammonia - metabolism</topic><topic>analytical methods</topic><topic>binding capacity</topic><topic>Biological and medical sciences</topic><topic>deamidation</topic><topic>disulfide bonds</topic><topic>electrostatic interactions</topic><topic>fluorescence</topic><topic>Fluorescent Dyes</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gels</topic><topic>Gels - chemistry</topic><topic>Glutaminase - metabolism</topic><topic>heat treatment</topic><topic>Hot Temperature</topic><topic>Milk and cheese industries. Ice creams</topic><topic>Milk Proteins - chemistry</topic><topic>Milk Proteins - metabolism</topic><topic>Molecular Weight</topic><topic>polymerization</topic><topic>Protein Conformation</topic><topic>salts</topic><topic>Spectrometry, Fluorescence</topic><topic>texture</topic><topic>water holding capacity</topic><topic>whey protein isolate</topic><topic>Whey Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miwa, Noriko</creatorcontrib><creatorcontrib>Yokoyama, Keiichi</creatorcontrib><creatorcontrib>Nio, Noriki</creatorcontrib><creatorcontrib>Sonomoto, Kenji</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><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>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miwa, Noriko</au><au>Yokoyama, Keiichi</au><au>Nio, Noriki</au><au>Sonomoto, Kenji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of Enzymatic Deamidation on the Heat-induced Conformational Changes in Whey Protein Isolate and Its Relation to Gel Properties</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2013-03-06</date><risdate>2013</risdate><volume>61</volume><issue>9</issue><spage>2205</spage><epage>2212</epage><pages>2205-2212</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The effect of protein-glutaminase (PG) on the heat-induced conformational changes in whey protein isolate (WPI) and its relation to gel properties was investigated. The structural properties of WPI treated with PG were examined by several analytical methods. The analysis of the fluorescence spectrum and the binding capacity of a fluorescent probe demonstrated that deamidation prevented the increase in the fluorescence intensity caused by subsequent heat treatment. Measurements of the molecular weight distribution of WPI showed that PG-treated WPI was not likely to polymerize even after heating. This is thought to be due to an increase in electrostatic repulsion between carboxylic acid groups and a decrease in the formation of disulfide bonds, which results in the decrease in heat-induced aggregation. The properties of heat-induced WPI gels were modified by deamidation. PG-treated WPI gels had a soft texture and a high water-holding capacity in the presence of salts.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>23379844</pmid><doi>10.1021/jf3047626</doi><tpages>8</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 2013-03, Vol.61 (9), p.2205-2212 |
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| subjects | Ammonia - metabolism analytical methods binding capacity Biological and medical sciences deamidation disulfide bonds electrostatic interactions fluorescence Fluorescent Dyes Food industries Fundamental and applied biological sciences. Psychology gels Gels - chemistry Glutaminase - metabolism heat treatment Hot Temperature Milk and cheese industries. Ice creams Milk Proteins - chemistry Milk Proteins - metabolism Molecular Weight polymerization Protein Conformation salts Spectrometry, Fluorescence texture water holding capacity whey protein isolate Whey Proteins |
| title | Effect of Enzymatic Deamidation on the Heat-induced Conformational Changes in Whey Protein Isolate and Its Relation to Gel Properties |
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