Proteolytic Activities of Suparen and Rennilase on Buffalo, Cow, and Goat Whole Casein and β-Casein
The proteolytic specificity and activity of Mucor miehei protease (Rennilase) and Endothia parasitica protease (Suparen) on buffalo, cow, and goat whole casein and β-casein (CN) were studied by analyzing the degradation products. The results suggest that Rennilase hydrolyzes casein of the three spec...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1999-09, Vol.47 (9), p.3632-3639 |
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| creator | Awad, S Lüthi-Peng, Qiao-Qian Puhan, Z |
| description | The proteolytic specificity and activity of Mucor miehei protease (Rennilase) and Endothia parasitica protease (Suparen) on buffalo, cow, and goat whole casein and β-casein (CN) were studied by analyzing the degradation products. The results suggest that Rennilase hydrolyzes casein of the three species in a manner similar to that of chymosin, resulting in the formation of αs1-I and β-I, -II, -III as initial degradation fragments of αs1- and β-CN. αs1-I was also the initial breakdown product of αs1-CN by Suparen. Contrary to Rennilase, Suparen showed a higher affinity toward β-CN and hydrolyzes β-CN, giving rise to degradation products characterized by mobility lower than that of β-CN. Increasing NaCl concentration (>3%) reduced the proteolysis of β-CN of the three species by Rennilase but not by Suparen. The hydrolysis of αs1-CN and αs1-I by the two enzymes was enhanced in the presence of NaCl. Keywords: Proteolysis; Suparen; Rennilase; buffalo, cow, goat caseins |
| doi_str_mv | 10.1021/jf981365u |
| format | Article |
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The results suggest that Rennilase hydrolyzes casein of the three species in a manner similar to that of chymosin, resulting in the formation of αs1-I and β-I, -II, -III as initial degradation fragments of αs1- and β-CN. αs1-I was also the initial breakdown product of αs1-CN by Suparen. Contrary to Rennilase, Suparen showed a higher affinity toward β-CN and hydrolyzes β-CN, giving rise to degradation products characterized by mobility lower than that of β-CN. Increasing NaCl concentration (>3%) reduced the proteolysis of β-CN of the three species by Rennilase but not by Suparen. The hydrolysis of αs1-CN and αs1-I by the two enzymes was enhanced in the presence of NaCl. Keywords: Proteolysis; Suparen; Rennilase; buffalo, cow, goat caseins</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf981365u</identifier><identifier>PMID: 10552696</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; Biological and medical sciences ; Buffaloes ; Caseins - metabolism ; Cattle ; Chymosin - metabolism ; Endopeptidases - metabolism ; Female ; Food industries ; Fundamental and applied biological sciences. Psychology ; Goats ; Hydrolysis ; Milk and cheese industries. Ice creams ; Protein Isoforms - metabolism</subject><ispartof>Journal of agricultural and food chemistry, 1999-09, Vol.47 (9), p.3632-3639</ispartof><rights>Copyright © 1999 American Chemical Society</rights><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a378t-9abf13c3e49766604a4a4d694d70628014faa985e74f5abb80f26739213df77c3</citedby><cites>FETCH-LOGICAL-a378t-9abf13c3e49766604a4a4d694d70628014faa985e74f5abb80f26739213df77c3</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/jf981365u$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf981365u$$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=1234791$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10552696$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Awad, S</creatorcontrib><creatorcontrib>Lüthi-Peng, Qiao-Qian</creatorcontrib><creatorcontrib>Puhan, Z</creatorcontrib><title>Proteolytic Activities of Suparen and Rennilase on Buffalo, Cow, and Goat Whole Casein and β-Casein</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>The proteolytic specificity and activity of Mucor miehei protease (Rennilase) and Endothia parasitica protease (Suparen) on buffalo, cow, and goat whole casein and β-casein (CN) were studied by analyzing the degradation products. The results suggest that Rennilase hydrolyzes casein of the three species in a manner similar to that of chymosin, resulting in the formation of αs1-I and β-I, -II, -III as initial degradation fragments of αs1- and β-CN. αs1-I was also the initial breakdown product of αs1-CN by Suparen. Contrary to Rennilase, Suparen showed a higher affinity toward β-CN and hydrolyzes β-CN, giving rise to degradation products characterized by mobility lower than that of β-CN. Increasing NaCl concentration (>3%) reduced the proteolysis of β-CN of the three species by Rennilase but not by Suparen. The hydrolysis of αs1-CN and αs1-I by the two enzymes was enhanced in the presence of NaCl. Keywords: Proteolysis; Suparen; Rennilase; buffalo, cow, goat caseins</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Buffaloes</subject><subject>Caseins - metabolism</subject><subject>Cattle</subject><subject>Chymosin - metabolism</subject><subject>Endopeptidases - metabolism</subject><subject>Female</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Goats</subject><subject>Hydrolysis</subject><subject>Milk and cheese industries. Ice creams</subject><subject>Protein Isoforms - metabolism</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M1uEzEQB3ALFdG0cOgLVD5QJKQs2Lvrr2MblUBUiYoG9WhNvLbqsFmn9i5tX4sH4ZkwbNRyqHywrPnNaPxH6IiSD5SU9OPaKUkrzoYXaEJZSQpGqdxDE5KLhWSc7qODlNaEEMkEeYX2KWGs5IpPUHMZQ29D-9B7g09N73_63tuEg8NXwxai7TB0Df5mu863kCwOHT4bnIM2TPEs3E3_lecBenx9E1qLZxn5sen3r2J8vUYvc0Oyb3b3Ifr-6Xw5-1xcfJ1_mZ1eFFAJ2RcKVo5WprK1EpxzUkM-DVd1IwgvJaG1A1CSWVE7BquVJK7kolIlrRonhKkO0btx7jaG28GmXm98MrZtobNhSJqrUnJJRYbvR2hiSClap7fRbyA-aEr030j1Y6TZHu-GDquNbf6TY4YZvN0BSAZaF6EzPj25sqqFopkVI_Opt_ePZYg_dP6EYHp5eaXnS3VN5oszvcj-ZPRgkl6HIXY5umf2-wM0YZhX</recordid><startdate>19990901</startdate><enddate>19990901</enddate><creator>Awad, S</creator><creator>Lüthi-Peng, Qiao-Qian</creator><creator>Puhan, Z</creator><general>American Chemical Society</general><scope>BSCLL</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>19990901</creationdate><title>Proteolytic Activities of Suparen and Rennilase on Buffalo, Cow, and Goat Whole Casein and β-Casein</title><author>Awad, S ; Lüthi-Peng, Qiao-Qian ; Puhan, Z</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a378t-9abf13c3e49766604a4a4d694d70628014faa985e74f5abb80f26739213df77c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Buffaloes</topic><topic>Caseins - metabolism</topic><topic>Cattle</topic><topic>Chymosin - metabolism</topic><topic>Endopeptidases - metabolism</topic><topic>Female</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Goats</topic><topic>Hydrolysis</topic><topic>Milk and cheese industries. Ice creams</topic><topic>Protein Isoforms - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Awad, S</creatorcontrib><creatorcontrib>Lüthi-Peng, Qiao-Qian</creatorcontrib><creatorcontrib>Puhan, Z</creatorcontrib><collection>Istex</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>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 Suparen and Rennilase on Buffalo, Cow, and Goat Whole Casein and β-Casein</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1999-09-01</date><risdate>1999</risdate><volume>47</volume><issue>9</issue><spage>3632</spage><epage>3639</epage><pages>3632-3639</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>The proteolytic specificity and activity of Mucor miehei protease (Rennilase) and Endothia parasitica protease (Suparen) on buffalo, cow, and goat whole casein and β-casein (CN) were studied by analyzing the degradation products. The results suggest that Rennilase hydrolyzes casein of the three species in a manner similar to that of chymosin, resulting in the formation of αs1-I and β-I, -II, -III as initial degradation fragments of αs1- and β-CN. αs1-I was also the initial breakdown product of αs1-CN by Suparen. Contrary to Rennilase, Suparen showed a higher affinity toward β-CN and hydrolyzes β-CN, giving rise to degradation products characterized by mobility lower than that of β-CN. Increasing NaCl concentration (>3%) reduced the proteolysis of β-CN of the three species by Rennilase but not by Suparen. The hydrolysis of αs1-CN and αs1-I by the two enzymes was enhanced in the presence of NaCl. Keywords: Proteolysis; Suparen; Rennilase; buffalo, cow, goat caseins</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>10552696</pmid><doi>10.1021/jf981365u</doi><tpages>8</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 1999-09, Vol.47 (9), p.3632-3639 |
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| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Animals Biological and medical sciences Buffaloes Caseins - metabolism Cattle Chymosin - metabolism Endopeptidases - metabolism Female Food industries Fundamental and applied biological sciences. Psychology Goats Hydrolysis Milk and cheese industries. Ice creams Protein Isoforms - metabolism |
| title | Proteolytic Activities of Suparen and Rennilase on Buffalo, Cow, and Goat Whole Casein and β-Casein |
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