Proteolytic Activities of Chymosin and Porcine Pepsin on Buffalo, Cow, and Goat Whole and β-Casein Fractions
The proteolytic specificity and activity of a recombinant chymosin (Maxiren) and porcine pepsin on buffalo, cow, and goat whole casein (CN) and β-CN were studied by analyzing the degradation products. The results suggest that the hydrolysis of whole casein of buffalo and goat by chymosin was similar...
Gespeichert in:
| Veröffentlicht in: | Journal of agricultural and food chemistry 1998-12, Vol.46 (12), p.4997-5007 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 5007 |
|---|---|
| container_issue | 12 |
| container_start_page | 4997 |
| container_title | Journal of agricultural and food chemistry |
| container_volume | 46 |
| creator | Awad, S Lüthi-Peng, Qiao-Qian Puhan, Z |
| description | The proteolytic specificity and activity of a recombinant chymosin (Maxiren) and porcine pepsin on buffalo, cow, and goat whole casein (CN) and β-CN were studied by analyzing the degradation products. The results suggest that the hydrolysis of whole casein of buffalo and goat by chymosin was similar to that of cow casein resulting in αs1-I and β-I, -II, and -III as degradation fragments of αs1- and β-CN. The exception was goat β-I which was resistant to further hydrolysis by chymosin but not to porcine pepsin at pH 5.4−6.2. Increasing NaCl concentration to ≥5% reduced the proteolysis of β-CN in all three species, but not that of αs1-CN. The fragments of β-I, -II, and -III produced from β-CN of the three species gave identical results with PAGE. αs1-I and its degradation fragments had in all three species, regardless of the different electrophoretic mobilities on PAGE, the same sequence of appearance. The results indicate that chymosin and porcine pepsin attacked in buffalo and goat caseins the same regions as known for cow αs1- and β-CN. Keywords: Proteolysis; chymosin; porcine pepsin; buffalo, cow, goat caseins |
| doi_str_mv | 10.1021/jf9804443 |
| format | Article |
| fullrecord | <record><control><sourceid>acs_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1021_jf9804443</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>c689313809</sourcerecordid><originalsourceid>FETCH-LOGICAL-a348t-a06a39105a5debc45173a65933f5a7b816846bcdacb12dede2b79b3a4b60cfa83</originalsourceid><addsrcrecordid>eNpt0M1u1DAQB3CrohJL4cAT4EM5IDUwjmPHOZaoH4hKRLQVUi_WxLGpt7vxyk4L-1p9kD4TboPKhZM_5jej0Z-Qtww-MijZp6VrFFRVxXfIgokSCsGYekEWkIuFEpK9JK9SWgKAEjUsyLqLYbJhtZ28oYdm8nd-8jbR4Gh7vV2H5EeK40C7EI0fLe3s5vErjPTzrXO4Cge0Db8OnsxJwIn-uA4r-_R8uC9aTDbr44h5chjTa7Kbe5J98_fcI5fHRxftaXH27eRLe3hWIK_UVCBI5A0DgWKwvakEqzlK0XDuBNa9YlJVsjcDmp6Vgx1s2ddNz7HqJRiHiu-RD_NcE0NK0Tq9iX6NcasZ6Mec9HNO2e7PdoPJ4MpFHI1P_xqkkBJkZsXMfJrs7-cyxhsta14LfdGd66uv-fq9VrrL_t3sHQaNP2MeeXleAuNQNiBKIbJ4Pws0SS_DbRxzJP9Z8A_xEow_</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Proteolytic Activities of Chymosin and Porcine Pepsin on Buffalo, Cow, and Goat Whole and β-Casein Fractions</title><source>ACS Publications</source><creator>Awad, S ; Lüthi-Peng, Qiao-Qian ; Puhan, Z</creator><creatorcontrib>Awad, S ; Lüthi-Peng, Qiao-Qian ; Puhan, Z</creatorcontrib><description>The proteolytic specificity and activity of a recombinant chymosin (Maxiren) and porcine pepsin on buffalo, cow, and goat whole casein (CN) and β-CN were studied by analyzing the degradation products. The results suggest that the hydrolysis of whole casein of buffalo and goat by chymosin was similar to that of cow casein resulting in αs1-I and β-I, -II, and -III as degradation fragments of αs1- and β-CN. The exception was goat β-I which was resistant to further hydrolysis by chymosin but not to porcine pepsin at pH 5.4−6.2. Increasing NaCl concentration to ≥5% reduced the proteolysis of β-CN in all three species, but not that of αs1-CN. The fragments of β-I, -II, and -III produced from β-CN of the three species gave identical results with PAGE. αs1-I and its degradation fragments had in all three species, regardless of the different electrophoretic mobilities on PAGE, the same sequence of appearance. The results indicate that chymosin and porcine pepsin attacked in buffalo and goat caseins the same regions as known for cow αs1- and β-CN. Keywords: Proteolysis; chymosin; porcine pepsin; buffalo, cow, goat caseins</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf9804443</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>beta-casein ; Biological and medical sciences ; buffalo milk ; casein ; cheesemaking ; chymosin ; Food industries ; Fundamental and applied biological sciences. Psychology ; goat milk ; hydrolysis ; milk ; Milk and cheese industries. Ice creams ; pepsin ; proteolysis ; recombinant chymosin ; recombinant proteins ; sodium chloride ; swine</subject><ispartof>Journal of agricultural and food chemistry, 1998-12, Vol.46 (12), p.4997-5007</ispartof><rights>Copyright © 1998 American Chemical Society</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a348t-a06a39105a5debc45173a65933f5a7b816846bcdacb12dede2b79b3a4b60cfa83</citedby><cites>FETCH-LOGICAL-a348t-a06a39105a5debc45173a65933f5a7b816846bcdacb12dede2b79b3a4b60cfa83</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/jf9804443$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf9804443$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2753,27058,27906,27907,56720,56770</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1656606$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Awad, S</creatorcontrib><creatorcontrib>Lüthi-Peng, Qiao-Qian</creatorcontrib><creatorcontrib>Puhan, Z</creatorcontrib><title>Proteolytic Activities of Chymosin and Porcine Pepsin on Buffalo, Cow, and Goat Whole and β-Casein Fractions</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The proteolytic specificity and activity of a recombinant chymosin (Maxiren) and porcine pepsin on buffalo, cow, and goat whole casein (CN) and β-CN were studied by analyzing the degradation products. The results suggest that the hydrolysis of whole casein of buffalo and goat by chymosin was similar to that of cow casein resulting in αs1-I and β-I, -II, and -III as degradation fragments of αs1- and β-CN. The exception was goat β-I which was resistant to further hydrolysis by chymosin but not to porcine pepsin at pH 5.4−6.2. Increasing NaCl concentration to ≥5% reduced the proteolysis of β-CN in all three species, but not that of αs1-CN. The fragments of β-I, -II, and -III produced from β-CN of the three species gave identical results with PAGE. αs1-I and its degradation fragments had in all three species, regardless of the different electrophoretic mobilities on PAGE, the same sequence of appearance. The results indicate that chymosin and porcine pepsin attacked in buffalo and goat caseins the same regions as known for cow αs1- and β-CN. Keywords: Proteolysis; chymosin; porcine pepsin; buffalo, cow, goat caseins</description><subject>beta-casein</subject><subject>Biological and medical sciences</subject><subject>buffalo milk</subject><subject>casein</subject><subject>cheesemaking</subject><subject>chymosin</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>goat milk</subject><subject>hydrolysis</subject><subject>milk</subject><subject>Milk and cheese industries. Ice creams</subject><subject>pepsin</subject><subject>proteolysis</subject><subject>recombinant chymosin</subject><subject>recombinant proteins</subject><subject>sodium chloride</subject><subject>swine</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNpt0M1u1DAQB3CrohJL4cAT4EM5IDUwjmPHOZaoH4hKRLQVUi_WxLGpt7vxyk4L-1p9kD4TboPKhZM_5jej0Z-Qtww-MijZp6VrFFRVxXfIgokSCsGYekEWkIuFEpK9JK9SWgKAEjUsyLqLYbJhtZ28oYdm8nd-8jbR4Gh7vV2H5EeK40C7EI0fLe3s5vErjPTzrXO4Cge0Db8OnsxJwIn-uA4r-_R8uC9aTDbr44h5chjTa7Kbe5J98_fcI5fHRxftaXH27eRLe3hWIK_UVCBI5A0DgWKwvakEqzlK0XDuBNa9YlJVsjcDmp6Vgx1s2ddNz7HqJRiHiu-RD_NcE0NK0Tq9iX6NcasZ6Mec9HNO2e7PdoPJ4MpFHI1P_xqkkBJkZsXMfJrs7-cyxhsta14LfdGd66uv-fq9VrrL_t3sHQaNP2MeeXleAuNQNiBKIbJ4Pws0SS_DbRxzJP9Z8A_xEow_</recordid><startdate>19981221</startdate><enddate>19981221</enddate><creator>Awad, S</creator><creator>Lüthi-Peng, Qiao-Qian</creator><creator>Puhan, Z</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19981221</creationdate><title>Proteolytic Activities of Chymosin and Porcine Pepsin on Buffalo, Cow, and Goat Whole and β-Casein Fractions</title><author>Awad, S ; Lüthi-Peng, Qiao-Qian ; Puhan, Z</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a348t-a06a39105a5debc45173a65933f5a7b816846bcdacb12dede2b79b3a4b60cfa83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>beta-casein</topic><topic>Biological and medical sciences</topic><topic>buffalo milk</topic><topic>casein</topic><topic>cheesemaking</topic><topic>chymosin</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>goat milk</topic><topic>hydrolysis</topic><topic>milk</topic><topic>Milk and cheese industries. Ice creams</topic><topic>pepsin</topic><topic>proteolysis</topic><topic>recombinant chymosin</topic><topic>recombinant proteins</topic><topic>sodium chloride</topic><topic>swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Awad, S</creatorcontrib><creatorcontrib>Lüthi-Peng, Qiao-Qian</creatorcontrib><creatorcontrib>Puhan, Z</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>Awad, S</au><au>Lüthi-Peng, Qiao-Qian</au><au>Puhan, Z</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteolytic Activities of Chymosin and Porcine Pepsin on Buffalo, Cow, and Goat Whole and β-Casein Fractions</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1998-12-21</date><risdate>1998</risdate><volume>46</volume><issue>12</issue><spage>4997</spage><epage>5007</epage><pages>4997-5007</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The proteolytic specificity and activity of a recombinant chymosin (Maxiren) and porcine pepsin on buffalo, cow, and goat whole casein (CN) and β-CN were studied by analyzing the degradation products. The results suggest that the hydrolysis of whole casein of buffalo and goat by chymosin was similar to that of cow casein resulting in αs1-I and β-I, -II, and -III as degradation fragments of αs1- and β-CN. The exception was goat β-I which was resistant to further hydrolysis by chymosin but not to porcine pepsin at pH 5.4−6.2. Increasing NaCl concentration to ≥5% reduced the proteolysis of β-CN in all three species, but not that of αs1-CN. The fragments of β-I, -II, and -III produced from β-CN of the three species gave identical results with PAGE. αs1-I and its degradation fragments had in all three species, regardless of the different electrophoretic mobilities on PAGE, the same sequence of appearance. The results indicate that chymosin and porcine pepsin attacked in buffalo and goat caseins the same regions as known for cow αs1- and β-CN. Keywords: Proteolysis; chymosin; porcine pepsin; buffalo, cow, goat caseins</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf9804443</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-8561 |
| ispartof | Journal of agricultural and food chemistry, 1998-12, Vol.46 (12), p.4997-5007 |
| issn | 0021-8561 1520-5118 |
| language | eng |
| recordid | cdi_crossref_primary_10_1021_jf9804443 |
| source | ACS Publications |
| subjects | beta-casein Biological and medical sciences buffalo milk casein cheesemaking chymosin Food industries Fundamental and applied biological sciences. Psychology goat milk hydrolysis milk Milk and cheese industries. Ice creams pepsin proteolysis recombinant chymosin recombinant proteins sodium chloride swine |
| title | Proteolytic Activities of Chymosin and Porcine Pepsin on Buffalo, Cow, and Goat Whole and β-Casein Fractions |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-17T09%3A57%3A38IST&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=Proteolytic%20Activities%20of%20Chymosin%20and%20Porcine%20Pepsin%20on%20Buffalo,%20Cow,%20and%20Goat%20Whole%20and%20%CE%B2-Casein%20Fractions&rft.jtitle=Journal%20of%20agricultural%20and%20food%20chemistry&rft.au=Awad,%20S&rft.date=1998-12-21&rft.volume=46&rft.issue=12&rft.spage=4997&rft.epage=5007&rft.pages=4997-5007&rft.issn=0021-8561&rft.eissn=1520-5118&rft.coden=JAFCAU&rft_id=info:doi/10.1021/jf9804443&rft_dat=%3Cacs_cross%3Ec689313809%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 |