Degradation of Myosin by Enzymes of the Digestive System: Comparison between Native and Oxidatively Cross-Linked Protein
We compared proteolysis of H2O2/hemin-cross-linked myosin and the native protein. Pepsin, trypsin, and chymotrypsin, representative enzymes of the mammalian digestive tract, and the plant enzyme papain were chosen as proteases. Under conditions which caused prominent degradation of the native myosin...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1996-07, Vol.44 (7), p.1641-1646 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Kamin-Belsky, Nurit Brillon, Addic A Arav, Ruth Shaklai, Nurith |
| description | We compared proteolysis of H2O2/hemin-cross-linked myosin and the native protein. Pepsin, trypsin, and chymotrypsin, representative enzymes of the mammalian digestive tract, and the plant enzyme papain were chosen as proteases. Under conditions which caused prominent degradation of the native myosin, only minimal degradation of the cross-linked protein was observed when individual enzymes were applied. Successive proteolysis by pepsin at gastric pH (1.85) followed by trypsin and chymotrypsin at duodenal pH (8.0) also showed retarded proteolysis of cross-linked myosin. At low pH both myosin forms precipitated, but by elevation of the pH only cross-linked myosin was partially resolubilized and the solubility was augmented following its minimal proteolytic degradation. It was concluded that although in general oxidatively modified proteins are susceptible to proteolysis, oxidatively cross-linked myosin is resistant. The data suggest that decreased digestibility of cross-linked myosin may lead to reduced quality of oxidized muscle foods. Keywords: Myosin; heme; peroxidation; cross-linking; proteolysis |
| doi_str_mv | 10.1021/jf950413x |
| format | Article |
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Pepsin, trypsin, and chymotrypsin, representative enzymes of the mammalian digestive tract, and the plant enzyme papain were chosen as proteases. Under conditions which caused prominent degradation of the native myosin, only minimal degradation of the cross-linked protein was observed when individual enzymes were applied. Successive proteolysis by pepsin at gastric pH (1.85) followed by trypsin and chymotrypsin at duodenal pH (8.0) also showed retarded proteolysis of cross-linked myosin. At low pH both myosin forms precipitated, but by elevation of the pH only cross-linked myosin was partially resolubilized and the solubility was augmented following its minimal proteolytic degradation. It was concluded that although in general oxidatively modified proteins are susceptible to proteolysis, oxidatively cross-linked myosin is resistant. The data suggest that decreased digestibility of cross-linked myosin may lead to reduced quality of oxidized muscle foods. Keywords: Myosin; heme; peroxidation; cross-linking; proteolysis</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf950413x</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>ABLANDAMIENTO ; ATTENDRISSEMENT ; Biological and medical sciences ; CHYMOTRYPSINE ; DIGESTIBILIDAD ; DIGESTIBILITE ; EXPERIMENTACION IN VITRO ; EXPERIMENTATION IN VITRO ; Food industries ; Fundamental and applied biological sciences. Psychology ; GLOBULINAS ; GLOBULINE ; HEMOGLOBINA ; HEMOGLOBINE ; Meat and meat product industries ; OXIDACION ; OXYDATION ; PAPAINA ; PAPAINE ; PEPSINA ; PEPSINE ; PROTEOLISIS ; PROTEOLYSE ; QUIMOTRIPSINA ; TRIPSINA ; TRYPSINE</subject><ispartof>Journal of agricultural and food chemistry, 1996-07, Vol.44 (7), p.1641-1646</ispartof><rights>Copyright © 1996 American Chemical Society</rights><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a343t-2125dfe90359bade5ef96330cbc8b8a93b255286a7f005a2fb49d6bfafd015fe3</citedby><cites>FETCH-LOGICAL-a343t-2125dfe90359bade5ef96330cbc8b8a93b255286a7f005a2fb49d6bfafd015fe3</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/jf950413x$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf950413x$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2751,27055,27903,27904,56716,56766</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3193016$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Kamin-Belsky, Nurit</creatorcontrib><creatorcontrib>Brillon, Addic A</creatorcontrib><creatorcontrib>Arav, Ruth</creatorcontrib><creatorcontrib>Shaklai, Nurith</creatorcontrib><title>Degradation of Myosin by Enzymes of the Digestive System: Comparison between Native and Oxidatively Cross-Linked Protein</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>We compared proteolysis of H2O2/hemin-cross-linked myosin and the native protein. Pepsin, trypsin, and chymotrypsin, representative enzymes of the mammalian digestive tract, and the plant enzyme papain were chosen as proteases. Under conditions which caused prominent degradation of the native myosin, only minimal degradation of the cross-linked protein was observed when individual enzymes were applied. Successive proteolysis by pepsin at gastric pH (1.85) followed by trypsin and chymotrypsin at duodenal pH (8.0) also showed retarded proteolysis of cross-linked myosin. At low pH both myosin forms precipitated, but by elevation of the pH only cross-linked myosin was partially resolubilized and the solubility was augmented following its minimal proteolytic degradation. It was concluded that although in general oxidatively modified proteins are susceptible to proteolysis, oxidatively cross-linked myosin is resistant. The data suggest that decreased digestibility of cross-linked myosin may lead to reduced quality of oxidized muscle foods. Keywords: Myosin; heme; peroxidation; cross-linking; proteolysis</description><subject>ABLANDAMIENTO</subject><subject>ATTENDRISSEMENT</subject><subject>Biological and medical sciences</subject><subject>CHYMOTRYPSINE</subject><subject>DIGESTIBILIDAD</subject><subject>DIGESTIBILITE</subject><subject>EXPERIMENTACION IN VITRO</subject><subject>EXPERIMENTATION IN VITRO</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GLOBULINAS</subject><subject>GLOBULINE</subject><subject>HEMOGLOBINA</subject><subject>HEMOGLOBINE</subject><subject>Meat and meat product industries</subject><subject>OXIDACION</subject><subject>OXYDATION</subject><subject>PAPAINA</subject><subject>PAPAINE</subject><subject>PEPSINA</subject><subject>PEPSINE</subject><subject>PROTEOLISIS</subject><subject>PROTEOLYSE</subject><subject>QUIMOTRIPSINA</subject><subject>TRIPSINA</subject><subject>TRYPSINE</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNptkLFu2zAQhokiBeqkHbp24tAMGdQeRVMSuwVykhawmwBKlizESSJdOjZlkGpjpUvXvmafpHRUeOp0uPu_Oxw-Qt4y-MAgZR9XRgqYMr57QSZMpJAIxoojMoEYJoXI2CtyHMIKAAqRw4T8nOmlxxZ72znaGboYumAdrQd64Z6GjQ77Yf9N05ld6tDbH5pWQ-j15tOfX79p2W226G2Iu7XuH7V29Cs-Q-haer2z7XO3HmjpuxCSuXUPuqU3vuu1da_JS4ProN_8qyfk7vLitvyczK-vvpTn8wT5lPdJylLRGi2BC1ljq4U2MuMcmrop6gIlr1Mh0iLD3AAITE09lW1WGzQtMGE0PyFn491m_4TXRm293aAfFAO1t6YO1iL7fmS3GBpcG4-useGwwJnkwLKIJSNmo4vdIUb_oLKc50Ld3lSqqO4X1ay8V4vIvxt5g53CZVSm7iqZg5CQxvB0DLEJatV99y7a-M9vfwEIk5L5</recordid><startdate>19960718</startdate><enddate>19960718</enddate><creator>Kamin-Belsky, Nurit</creator><creator>Brillon, Addic A</creator><creator>Arav, Ruth</creator><creator>Shaklai, Nurith</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19960718</creationdate><title>Degradation of Myosin by Enzymes of the Digestive System: Comparison between Native and Oxidatively Cross-Linked Protein</title><author>Kamin-Belsky, Nurit ; Brillon, Addic A ; Arav, Ruth ; Shaklai, Nurith</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a343t-2125dfe90359bade5ef96330cbc8b8a93b255286a7f005a2fb49d6bfafd015fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>ABLANDAMIENTO</topic><topic>ATTENDRISSEMENT</topic><topic>Biological and medical sciences</topic><topic>CHYMOTRYPSINE</topic><topic>DIGESTIBILIDAD</topic><topic>DIGESTIBILITE</topic><topic>EXPERIMENTACION IN VITRO</topic><topic>EXPERIMENTATION IN VITRO</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GLOBULINAS</topic><topic>GLOBULINE</topic><topic>HEMOGLOBINA</topic><topic>HEMOGLOBINE</topic><topic>Meat and meat product industries</topic><topic>OXIDACION</topic><topic>OXYDATION</topic><topic>PAPAINA</topic><topic>PAPAINE</topic><topic>PEPSINA</topic><topic>PEPSINE</topic><topic>PROTEOLISIS</topic><topic>PROTEOLYSE</topic><topic>QUIMOTRIPSINA</topic><topic>TRIPSINA</topic><topic>TRYPSINE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kamin-Belsky, Nurit</creatorcontrib><creatorcontrib>Brillon, Addic A</creatorcontrib><creatorcontrib>Arav, Ruth</creatorcontrib><creatorcontrib>Shaklai, Nurith</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>Kamin-Belsky, Nurit</au><au>Brillon, Addic A</au><au>Arav, Ruth</au><au>Shaklai, Nurith</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Degradation of Myosin by Enzymes of the Digestive System: Comparison between Native and Oxidatively Cross-Linked Protein</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1996-07-18</date><risdate>1996</risdate><volume>44</volume><issue>7</issue><spage>1641</spage><epage>1646</epage><pages>1641-1646</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>We compared proteolysis of H2O2/hemin-cross-linked myosin and the native protein. Pepsin, trypsin, and chymotrypsin, representative enzymes of the mammalian digestive tract, and the plant enzyme papain were chosen as proteases. Under conditions which caused prominent degradation of the native myosin, only minimal degradation of the cross-linked protein was observed when individual enzymes were applied. Successive proteolysis by pepsin at gastric pH (1.85) followed by trypsin and chymotrypsin at duodenal pH (8.0) also showed retarded proteolysis of cross-linked myosin. At low pH both myosin forms precipitated, but by elevation of the pH only cross-linked myosin was partially resolubilized and the solubility was augmented following its minimal proteolytic degradation. It was concluded that although in general oxidatively modified proteins are susceptible to proteolysis, oxidatively cross-linked myosin is resistant. The data suggest that decreased digestibility of cross-linked myosin may lead to reduced quality of oxidized muscle foods. Keywords: Myosin; heme; peroxidation; cross-linking; proteolysis</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf950413x</doi><tpages>6</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 1996-07, Vol.44 (7), p.1641-1646 |
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| language | eng |
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| source | ACS Publications |
| subjects | ABLANDAMIENTO ATTENDRISSEMENT Biological and medical sciences CHYMOTRYPSINE DIGESTIBILIDAD DIGESTIBILITE EXPERIMENTACION IN VITRO EXPERIMENTATION IN VITRO Food industries Fundamental and applied biological sciences. Psychology GLOBULINAS GLOBULINE HEMOGLOBINA HEMOGLOBINE Meat and meat product industries OXIDACION OXYDATION PAPAINA PAPAINE PEPSINA PEPSINE PROTEOLISIS PROTEOLYSE QUIMOTRIPSINA TRIPSINA TRYPSINE |
| title | Degradation of Myosin by Enzymes of the Digestive System: Comparison between Native and Oxidatively Cross-Linked Protein |
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