Gelation of .beta.-lactoglobulin treated with limited proteolysis by immobilized trypsin
The gelation of beta-lactoglobulin treated by limited proteolysis with immobilized trypsin was studied by dynamic rheometry. Gelation conditions were (1) 80 degrees C for 3 h with 7% protein (w/v) in 20 mM CaCl2 at PH 7 and (2) 60 C for 12 h with 7 % (or 15 %) protein (w/v) in 20 mM CACl2 (or 100 mM...
Gespeichert in:
| Veröffentlicht in: | Journal of agricultural and food chemistry 1994-02, Vol.42 (2), p.234-239 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 239 |
|---|---|
| container_issue | 2 |
| container_start_page | 234 |
| container_title | Journal of agricultural and food chemistry |
| container_volume | 42 |
| creator | Chen, Sharon X Swaisgood, Harold E Foegeding, E. Allen |
| description | The gelation of beta-lactoglobulin treated by limited proteolysis with immobilized trypsin was studied by dynamic rheometry. Gelation conditions were (1) 80 degrees C for 3 h with 7% protein (w/v) in 20 mM CaCl2 at PH 7 and (2) 60 C for 12 h with 7 % (or 15 %) protein (w/v) in 20 mM CACl2 (or 100 mM NACl) at pH 7. Thermal transition temperatures of the different components in the limited proteolysis mixture were determined by differential scanning calorimetry to be 54.0, 58.8, 64.0, and 81.8 C, which are believed to correspond to fragments of the beta-barrel domain and native beta-lactoglobulin. The partially hydrolyzed beta-lactoglobulin had a lower gel point and gelled more rapidly than native beta-lactoglobulin at 80 C. Hydrolyzed beta-lactoglobulin, heated at 60 degrees C in 20 mM CaCl2, formed a weak gel at 7% (w/v) protein and a strong gel at 15% (w/v). By comparison, very weak gels were formed with native beta-lactoglobulin at both 7% and 15% (w/v) protein at 60 degrees C |
| doi_str_mv | 10.1021/jf00038a002 |
| format | Article |
| fullrecord | <record><control><sourceid>acs_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1021_jf00038a002</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>c931002598</sourcerecordid><originalsourceid>FETCH-LOGICAL-a349t-d1868849a0a70d8263d9027a27e6dad230c7e0fd36377fd33b8230d4cf3cc3ac3</originalsourceid><addsrcrecordid>eNptkM1LxDAQxYMouH6cvHnqQfAgXSdN26RHWfwCxQUVvIVpmmrWbLMkEV3_eiMV8eBpmPd-8xgeIQcUphQKerroAYAJBCg2yIRWBeQVpWKTTJJCc1HVdJvshLBImKg4TMjTpbYYjRsy12fTVkec5hZVdM_WtW_WDFn0GqPusncTXzJrluZ7WXkXtbPrYELWrjOzXLrWWPOZrOjXq2CGPbLVow16_2fukseL84fZVX5zd3k9O7vJkZVNzDsqaiHKBgE5dKKoWddAwbHguu6wKxgorqHvWM04T4O1ImldqXqmFEPFdsnJmKu8C8HrXq68WaJfSwryuxT5p5REH430CoNC23sclAm_JyWFqm6ahOUjZkLUH782-ldZc8Yr-TC_lxflrJzfzkt5lfjDke_RSXz2KfLxvqmgKgVN5vFoogpy4d78kPr497svPiSFzQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Gelation of .beta.-lactoglobulin treated with limited proteolysis by immobilized trypsin</title><source>American Chemical Society Journals</source><creator>Chen, Sharon X ; Swaisgood, Harold E ; Foegeding, E. Allen</creator><creatorcontrib>Chen, Sharon X ; Swaisgood, Harold E ; Foegeding, E. Allen</creatorcontrib><description>The gelation of beta-lactoglobulin treated by limited proteolysis with immobilized trypsin was studied by dynamic rheometry. Gelation conditions were (1) 80 degrees C for 3 h with 7% protein (w/v) in 20 mM CaCl2 at PH 7 and (2) 60 C for 12 h with 7 % (or 15 %) protein (w/v) in 20 mM CACl2 (or 100 mM NACl) at pH 7. Thermal transition temperatures of the different components in the limited proteolysis mixture were determined by differential scanning calorimetry to be 54.0, 58.8, 64.0, and 81.8 C, which are believed to correspond to fragments of the beta-barrel domain and native beta-lactoglobulin. The partially hydrolyzed beta-lactoglobulin had a lower gel point and gelled more rapidly than native beta-lactoglobulin at 80 C. Hydrolyzed beta-lactoglobulin, heated at 60 degrees C in 20 mM CaCl2, formed a weak gel at 7% (w/v) protein and a strong gel at 15% (w/v). By comparison, very weak gels were formed with native beta-lactoglobulin at both 7% and 15% (w/v) protein at 60 degrees C</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf00038a002</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts ; BETA LACTOGLOBULINA ; BETA LACTOGLOBULINE ; Biological and medical sciences ; Food industries ; Fundamental and applied biological sciences. Psychology ; GELIFICACION ; GELIFICATION ; IMMOBILISATION ; INMOVILIZACION ; PROPIEDADES REOLOGICAS ; PROPRIETE RHEOLOGIQUE ; PROTEOLISIS ; PROTEOLYSE ; TRIPSINA ; TRYPSINE</subject><ispartof>Journal of agricultural and food chemistry, 1994-02, Vol.42 (2), p.234-239</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a349t-d1868849a0a70d8263d9027a27e6dad230c7e0fd36377fd33b8230d4cf3cc3ac3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf00038a002$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf00038a002$$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=4105699$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Sharon X</creatorcontrib><creatorcontrib>Swaisgood, Harold E</creatorcontrib><creatorcontrib>Foegeding, E. Allen</creatorcontrib><title>Gelation of .beta.-lactoglobulin treated with limited proteolysis by immobilized trypsin</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The gelation of beta-lactoglobulin treated by limited proteolysis with immobilized trypsin was studied by dynamic rheometry. Gelation conditions were (1) 80 degrees C for 3 h with 7% protein (w/v) in 20 mM CaCl2 at PH 7 and (2) 60 C for 12 h with 7 % (or 15 %) protein (w/v) in 20 mM CACl2 (or 100 mM NACl) at pH 7. Thermal transition temperatures of the different components in the limited proteolysis mixture were determined by differential scanning calorimetry to be 54.0, 58.8, 64.0, and 81.8 C, which are believed to correspond to fragments of the beta-barrel domain and native beta-lactoglobulin. The partially hydrolyzed beta-lactoglobulin had a lower gel point and gelled more rapidly than native beta-lactoglobulin at 80 C. Hydrolyzed beta-lactoglobulin, heated at 60 degrees C in 20 mM CaCl2, formed a weak gel at 7% (w/v) protein and a strong gel at 15% (w/v). By comparison, very weak gels were formed with native beta-lactoglobulin at both 7% and 15% (w/v) protein at 60 degrees C</description><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>BETA LACTOGLOBULINA</subject><subject>BETA LACTOGLOBULINE</subject><subject>Biological and medical sciences</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GELIFICACION</subject><subject>GELIFICATION</subject><subject>IMMOBILISATION</subject><subject>INMOVILIZACION</subject><subject>PROPIEDADES REOLOGICAS</subject><subject>PROPRIETE RHEOLOGIQUE</subject><subject>PROTEOLISIS</subject><subject>PROTEOLYSE</subject><subject>TRIPSINA</subject><subject>TRYPSINE</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNptkM1LxDAQxYMouH6cvHnqQfAgXSdN26RHWfwCxQUVvIVpmmrWbLMkEV3_eiMV8eBpmPd-8xgeIQcUphQKerroAYAJBCg2yIRWBeQVpWKTTJJCc1HVdJvshLBImKg4TMjTpbYYjRsy12fTVkec5hZVdM_WtW_WDFn0GqPusncTXzJrluZ7WXkXtbPrYELWrjOzXLrWWPOZrOjXq2CGPbLVow16_2fukseL84fZVX5zd3k9O7vJkZVNzDsqaiHKBgE5dKKoWddAwbHguu6wKxgorqHvWM04T4O1ImldqXqmFEPFdsnJmKu8C8HrXq68WaJfSwryuxT5p5REH430CoNC23sclAm_JyWFqm6ahOUjZkLUH782-ldZc8Yr-TC_lxflrJzfzkt5lfjDke_RSXz2KfLxvqmgKgVN5vFoogpy4d78kPr497svPiSFzQ</recordid><startdate>19940201</startdate><enddate>19940201</enddate><creator>Chen, Sharon X</creator><creator>Swaisgood, Harold E</creator><creator>Foegeding, E. Allen</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19940201</creationdate><title>Gelation of .beta.-lactoglobulin treated with limited proteolysis by immobilized trypsin</title><author>Chen, Sharon X ; Swaisgood, Harold E ; Foegeding, E. Allen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a349t-d1868849a0a70d8263d9027a27e6dad230c7e0fd36377fd33b8230d4cf3cc3ac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</topic><topic>BETA LACTOGLOBULINA</topic><topic>BETA LACTOGLOBULINE</topic><topic>Biological and medical sciences</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GELIFICACION</topic><topic>GELIFICATION</topic><topic>IMMOBILISATION</topic><topic>INMOVILIZACION</topic><topic>PROPIEDADES REOLOGICAS</topic><topic>PROPRIETE RHEOLOGIQUE</topic><topic>PROTEOLISIS</topic><topic>PROTEOLYSE</topic><topic>TRIPSINA</topic><topic>TRYPSINE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Sharon X</creatorcontrib><creatorcontrib>Swaisgood, Harold E</creatorcontrib><creatorcontrib>Foegeding, E. Allen</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Sharon X</au><au>Swaisgood, Harold E</au><au>Foegeding, E. Allen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gelation of .beta.-lactoglobulin treated with limited proteolysis by immobilized trypsin</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1994-02-01</date><risdate>1994</risdate><volume>42</volume><issue>2</issue><spage>234</spage><epage>239</epage><pages>234-239</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The gelation of beta-lactoglobulin treated by limited proteolysis with immobilized trypsin was studied by dynamic rheometry. Gelation conditions were (1) 80 degrees C for 3 h with 7% protein (w/v) in 20 mM CaCl2 at PH 7 and (2) 60 C for 12 h with 7 % (or 15 %) protein (w/v) in 20 mM CACl2 (or 100 mM NACl) at pH 7. Thermal transition temperatures of the different components in the limited proteolysis mixture were determined by differential scanning calorimetry to be 54.0, 58.8, 64.0, and 81.8 C, which are believed to correspond to fragments of the beta-barrel domain and native beta-lactoglobulin. The partially hydrolyzed beta-lactoglobulin had a lower gel point and gelled more rapidly than native beta-lactoglobulin at 80 C. Hydrolyzed beta-lactoglobulin, heated at 60 degrees C in 20 mM CaCl2, formed a weak gel at 7% (w/v) protein and a strong gel at 15% (w/v). By comparison, very weak gels were formed with native beta-lactoglobulin at both 7% and 15% (w/v) protein at 60 degrees C</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf00038a002</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-8561 |
| ispartof | Journal of agricultural and food chemistry, 1994-02, Vol.42 (2), p.234-239 |
| issn | 0021-8561 1520-5118 |
| language | eng |
| recordid | cdi_crossref_primary_10_1021_jf00038a002 |
| source | American Chemical Society Journals |
| subjects | Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts BETA LACTOGLOBULINA BETA LACTOGLOBULINE Biological and medical sciences Food industries Fundamental and applied biological sciences. Psychology GELIFICACION GELIFICATION IMMOBILISATION INMOVILIZACION PROPIEDADES REOLOGICAS PROPRIETE RHEOLOGIQUE PROTEOLISIS PROTEOLYSE TRIPSINA TRYPSINE |
| title | Gelation of .beta.-lactoglobulin treated with limited proteolysis by immobilized trypsin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T16%3A31%3A46IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-acs_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Gelation%20of%20.beta.-lactoglobulin%20treated%20with%20limited%20proteolysis%20by%20immobilized%20trypsin&rft.jtitle=Journal%20of%20agricultural%20and%20food%20chemistry&rft.au=Chen,%20Sharon%20X&rft.date=1994-02-01&rft.volume=42&rft.issue=2&rft.spage=234&rft.epage=239&rft.pages=234-239&rft.issn=0021-8561&rft.eissn=1520-5118&rft.coden=JAFCAU&rft_id=info:doi/10.1021/jf00038a002&rft_dat=%3Cacs_cross%3Ec931002598%3C/acs_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |