Potential of Peroxynitrite To Alter the Color of Myoglobin in Muscle Foods
Superoxide anion and nitric oxide can react to form the highly oxidizing species peroxynitrite. The objective of this research was to determine if peroxynitrite can promote the discoloration of myoglobin under conditions expected in muscle foods. Reagent peroxynitrite (25−100 μM) caused rapid and ex...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2002-08, Vol.50 (18), p.5220-5223 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Connolly, Brian J Brannan, Robert G Decker, Eric A |
| description | Superoxide anion and nitric oxide can react to form the highly oxidizing species peroxynitrite. The objective of this research was to determine if peroxynitrite can promote the discoloration of myoglobin under conditions expected in muscle foods. Reagent peroxynitrite (25−100 μM) caused rapid and extensive formation of metmyoglobin from oxymyoglobin with the majority of metmyoglobin formation occurring during the first 5−10 min of incubation. Carbon dioxide caused a small decrease in the ability of peroxynitrite to oxidize oxymyoglobin, and peroxynitrite-promoted conversion of oxymyoglobin to metmyoglobin increased with decreasing pH (5.5−7.0). Differential scanning calorimetry suggested that peroxynitrite caused minimal changes in myoglobin structure. These results indicate that peroxynitrite can promote the conversion of oxymyoglobin to metmyoglobin under the conditions expected in muscle foods. Keywords: Myoglobin; meat color; peroxynitrite; nitric oxide; metmyoglobin |
| doi_str_mv | 10.1021/jf020289z |
| format | Article |
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The objective of this research was to determine if peroxynitrite can promote the discoloration of myoglobin under conditions expected in muscle foods. Reagent peroxynitrite (25−100 μM) caused rapid and extensive formation of metmyoglobin from oxymyoglobin with the majority of metmyoglobin formation occurring during the first 5−10 min of incubation. Carbon dioxide caused a small decrease in the ability of peroxynitrite to oxidize oxymyoglobin, and peroxynitrite-promoted conversion of oxymyoglobin to metmyoglobin increased with decreasing pH (5.5−7.0). Differential scanning calorimetry suggested that peroxynitrite caused minimal changes in myoglobin structure. These results indicate that peroxynitrite can promote the conversion of oxymyoglobin to metmyoglobin under the conditions expected in muscle foods. 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Psychology ; Hydrogen-Ion Concentration ; Kinetics ; Lipid Peroxidation ; Meat - analysis ; Meat and meat product industries ; Metmyoglobin - chemistry ; Muscle, Skeletal - chemistry ; Myoglobin - analysis ; Myoglobin - chemistry ; Peroxynitrous Acid - pharmacology ; Thermodynamics</subject><ispartof>Journal of agricultural and food chemistry, 2002-08, Vol.50 (18), p.5220-5223</ispartof><rights>Copyright © 2002 American Chemical Society</rights><rights>2002 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a379t-f324aeb5358acdd21bdeeed5c422a5e07ad0fa95590e4455f18f737942d80d763</citedby><cites>FETCH-LOGICAL-a379t-f324aeb5358acdd21bdeeed5c422a5e07ad0fa95590e4455f18f737942d80d763</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/jf020289z$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf020289z$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>315,781,785,2766,27078,27926,27927,56740,56790</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13877835$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12188633$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Connolly, Brian J</creatorcontrib><creatorcontrib>Brannan, Robert G</creatorcontrib><creatorcontrib>Decker, Eric A</creatorcontrib><title>Potential of Peroxynitrite To Alter the Color of Myoglobin in Muscle Foods</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Superoxide anion and nitric oxide can react to form the highly oxidizing species peroxynitrite. The objective of this research was to determine if peroxynitrite can promote the discoloration of myoglobin under conditions expected in muscle foods. Reagent peroxynitrite (25−100 μM) caused rapid and extensive formation of metmyoglobin from oxymyoglobin with the majority of metmyoglobin formation occurring during the first 5−10 min of incubation. Carbon dioxide caused a small decrease in the ability of peroxynitrite to oxidize oxymyoglobin, and peroxynitrite-promoted conversion of oxymyoglobin to metmyoglobin increased with decreasing pH (5.5−7.0). Differential scanning calorimetry suggested that peroxynitrite caused minimal changes in myoglobin structure. These results indicate that peroxynitrite can promote the conversion of oxymyoglobin to metmyoglobin under the conditions expected in muscle foods. Keywords: Myoglobin; meat color; peroxynitrite; nitric oxide; metmyoglobin</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calorimetry, Differential Scanning</subject><subject>Color</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Lipid Peroxidation</subject><subject>Meat - analysis</subject><subject>Meat and meat product industries</subject><subject>Metmyoglobin - chemistry</subject><subject>Muscle, Skeletal - chemistry</subject><subject>Myoglobin - analysis</subject><subject>Myoglobin - chemistry</subject><subject>Peroxynitrous Acid - pharmacology</subject><subject>Thermodynamics</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0E1LKzEUBuAgV7R-LPwDMpsruBg9yUw6maUU6wcWK9Z1SCcn905NJ5pkwPrrjbTYjRDI4jx5yXkJOaFwQYHRy4UBBkzUnztkQDmDnFMq_pABpGEu-JDuk4MQFgAgeAV7ZJ8yKsSwKAbkfuoidrFVNnMmm6J3H6uujb6NmM1cdmUj-iz-x2zkrPPfZrJy_6ybt12WzqQPjcVs7JwOR2TXKBvweHMfkpfx9Wx0mz883tyNrh5yVVR1zE3BSoVzXnChGq0ZnWtE1LwpGVMcoVIajKo5rwHLknNDhanSy5JpAboaFofkbJ375t17jyHKZRsatFZ16PogKwaUcQEJnq9h410IHo188-1S-ZWkIL-Lkz_FJXu6Ce3nS9RbuWkqgb8boEKjrPGqa9qwdYWoKlHw5PK1a0PEj5-58q9ymNbgcjZ9lvVNCU98MpXjba5qgly43nepu18--AVrlY_W</recordid><startdate>20020828</startdate><enddate>20020828</enddate><creator>Connolly, Brian J</creator><creator>Brannan, Robert G</creator><creator>Decker, Eric A</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>20020828</creationdate><title>Potential of Peroxynitrite To Alter the Color of Myoglobin in Muscle Foods</title><author>Connolly, Brian J ; Brannan, Robert G ; Decker, Eric A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a379t-f324aeb5358acdd21bdeeed5c422a5e07ad0fa95590e4455f18f737942d80d763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calorimetry, Differential Scanning</topic><topic>Color</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Lipid Peroxidation</topic><topic>Meat - analysis</topic><topic>Meat and meat product industries</topic><topic>Metmyoglobin - chemistry</topic><topic>Muscle, Skeletal - chemistry</topic><topic>Myoglobin - analysis</topic><topic>Myoglobin - chemistry</topic><topic>Peroxynitrous Acid - pharmacology</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Connolly, Brian J</creatorcontrib><creatorcontrib>Brannan, Robert G</creatorcontrib><creatorcontrib>Decker, Eric A</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>Connolly, Brian J</au><au>Brannan, Robert G</au><au>Decker, Eric A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Potential of Peroxynitrite To Alter the Color of Myoglobin in Muscle Foods</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2002-08-28</date><risdate>2002</risdate><volume>50</volume><issue>18</issue><spage>5220</spage><epage>5223</epage><pages>5220-5223</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Superoxide anion and nitric oxide can react to form the highly oxidizing species peroxynitrite. The objective of this research was to determine if peroxynitrite can promote the discoloration of myoglobin under conditions expected in muscle foods. Reagent peroxynitrite (25−100 μM) caused rapid and extensive formation of metmyoglobin from oxymyoglobin with the majority of metmyoglobin formation occurring during the first 5−10 min of incubation. Carbon dioxide caused a small decrease in the ability of peroxynitrite to oxidize oxymyoglobin, and peroxynitrite-promoted conversion of oxymyoglobin to metmyoglobin increased with decreasing pH (5.5−7.0). Differential scanning calorimetry suggested that peroxynitrite caused minimal changes in myoglobin structure. These results indicate that peroxynitrite can promote the conversion of oxymyoglobin to metmyoglobin under the conditions expected in muscle foods. Keywords: Myoglobin; meat color; peroxynitrite; nitric oxide; metmyoglobin</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>12188633</pmid><doi>10.1021/jf020289z</doi><tpages>4</tpages></addata></record> |
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| subjects | Animals Biological and medical sciences Calorimetry, Differential Scanning Color Food industries Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Kinetics Lipid Peroxidation Meat - analysis Meat and meat product industries Metmyoglobin - chemistry Muscle, Skeletal - chemistry Myoglobin - analysis Myoglobin - chemistry Peroxynitrous Acid - pharmacology Thermodynamics |
| title | Potential of Peroxynitrite To Alter the Color of Myoglobin in Muscle Foods |
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