Properties of Tilapia Carboxy- and Oxyhemoglobin at Postmortem pH
Hemoglobin plays an important role in the color and oxidative stability of seafoods. A recent practice in the seafood industry is to stabilize muscle color by the application of gases containing carbon monoxide. The goal of this study was to examine and compare the properties of tilapia hemoglobin c...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2005-05, Vol.53 (9), p.3643-3649 |
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| creator | Kristinsson, Hordur G Mony, Swapna S Petty, Holly T |
| description | Hemoglobin plays an important role in the color and oxidative stability of seafoods. A recent practice in the seafood industry is to stabilize muscle color by the application of gases containing carbon monoxide. The goal of this study was to examine and compare the properties of tilapia hemoglobin complexed to either O2 (Oxy-Hb) or CO (CO-Hb) at pH 6.5, which reflects the tilapia muscle postmortem pH. CO-Hb was significantly (p < 0.01) more stable against autoxidation compared to Oxy-Hb when kept at 4 and −30 °C for 23 days. Almost no loss of CO was detected for both temperatures according to the UV−vis spectra of Hb. This stabilization was also believed to play a role in increased protein structure stabilization (p < 0.001) since less protein aggregation was seen for CO-Hb. The higher protein stabilization for Hb was linked to the heme group, which was maintained in its reduced state longer for CO-Hb vs Oxy-Hb and was likely less exposed to solvent. CO-Hb had significantly (p < 0.01) less peroxidase activity than Oxy-Hb and thus reactivity with H2O2. The pro-oxidative activity of CO-Hb was significantly (p < 0.01) reduced in a linoleic acid micelle system compared to that of Oxy-Hb, while smaller differences in activity were seen in a washed cod and tilapia muscle model system. Keywords: Hemoglobin; tilapia; CO (carbon monoxide); O2 (oxygen); autoxidation; stability; peroxidase; pro-oxidative; lipid oxidation |
| doi_str_mv | 10.1021/jf048107j |
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A recent practice in the seafood industry is to stabilize muscle color by the application of gases containing carbon monoxide. The goal of this study was to examine and compare the properties of tilapia hemoglobin complexed to either O2 (Oxy-Hb) or CO (CO-Hb) at pH 6.5, which reflects the tilapia muscle postmortem pH. CO-Hb was significantly (p < 0.01) more stable against autoxidation compared to Oxy-Hb when kept at 4 and −30 °C for 23 days. Almost no loss of CO was detected for both temperatures according to the UV−vis spectra of Hb. This stabilization was also believed to play a role in increased protein structure stabilization (p < 0.001) since less protein aggregation was seen for CO-Hb. The higher protein stabilization for Hb was linked to the heme group, which was maintained in its reduced state longer for CO-Hb vs Oxy-Hb and was likely less exposed to solvent. CO-Hb had significantly (p < 0.01) less peroxidase activity than Oxy-Hb and thus reactivity with H2O2. The pro-oxidative activity of CO-Hb was significantly (p < 0.01) reduced in a linoleic acid micelle system compared to that of Oxy-Hb, while smaller differences in activity were seen in a washed cod and tilapia muscle model system. Keywords: Hemoglobin; tilapia; CO (carbon monoxide); O2 (oxygen); autoxidation; stability; peroxidase; pro-oxidative; lipid oxidation</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf048107j</identifier><identifier>PMID: 15853414</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; autoxidation ; Biological and medical sciences ; carbon monoxide ; carboxyhemoglobin ; Carboxyhemoglobin - chemistry ; Carboxyhemoglobin - metabolism ; Drug Stability ; enzyme activity ; Fish and seafood industries ; fish fillets ; Food industries ; food processing ; Fundamental and applied biological sciences. Psychology ; hemoglobin ; Hydrogen Peroxide - metabolism ; Hydrogen-Ion Concentration ; Oreochromis niloticus ; oxyhemoglobin ; Oxyhemoglobins - chemistry ; Oxyhemoglobins - metabolism ; peroxidase ; Peroxidase - metabolism ; Postmortem Changes ; protein aggregates ; skeletal muscle ; Spectrophotometry, Ultraviolet ; tilapia (common name) ; Tilapia - blood</subject><ispartof>Journal of agricultural and food chemistry, 2005-05, Vol.53 (9), p.3643-3649</ispartof><rights>Copyright © 2005 American Chemical Society</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a436t-85d439326a6fefa78cc50825b729eb4036f112f2f928b23ac81e305ef8d3cb253</citedby><cites>FETCH-LOGICAL-a436t-85d439326a6fefa78cc50825b729eb4036f112f2f928b23ac81e305ef8d3cb253</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/jf048107j$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf048107j$$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=16732698$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15853414$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kristinsson, Hordur G</creatorcontrib><creatorcontrib>Mony, Swapna S</creatorcontrib><creatorcontrib>Petty, Holly T</creatorcontrib><title>Properties of Tilapia Carboxy- and Oxyhemoglobin at Postmortem pH</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Hemoglobin plays an important role in the color and oxidative stability of seafoods. A recent practice in the seafood industry is to stabilize muscle color by the application of gases containing carbon monoxide. The goal of this study was to examine and compare the properties of tilapia hemoglobin complexed to either O2 (Oxy-Hb) or CO (CO-Hb) at pH 6.5, which reflects the tilapia muscle postmortem pH. CO-Hb was significantly (p < 0.01) more stable against autoxidation compared to Oxy-Hb when kept at 4 and −30 °C for 23 days. Almost no loss of CO was detected for both temperatures according to the UV−vis spectra of Hb. This stabilization was also believed to play a role in increased protein structure stabilization (p < 0.001) since less protein aggregation was seen for CO-Hb. The higher protein stabilization for Hb was linked to the heme group, which was maintained in its reduced state longer for CO-Hb vs Oxy-Hb and was likely less exposed to solvent. CO-Hb had significantly (p < 0.01) less peroxidase activity than Oxy-Hb and thus reactivity with H2O2. The pro-oxidative activity of CO-Hb was significantly (p < 0.01) reduced in a linoleic acid micelle system compared to that of Oxy-Hb, while smaller differences in activity were seen in a washed cod and tilapia muscle model system. Keywords: Hemoglobin; tilapia; CO (carbon monoxide); O2 (oxygen); autoxidation; stability; peroxidase; pro-oxidative; lipid oxidation</description><subject>Animals</subject><subject>autoxidation</subject><subject>Biological and medical sciences</subject><subject>carbon monoxide</subject><subject>carboxyhemoglobin</subject><subject>Carboxyhemoglobin - chemistry</subject><subject>Carboxyhemoglobin - metabolism</subject><subject>Drug Stability</subject><subject>enzyme activity</subject><subject>Fish and seafood industries</subject><subject>fish fillets</subject><subject>Food industries</subject><subject>food processing</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hemoglobin</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Hydrogen-Ion Concentration</subject><subject>Oreochromis niloticus</subject><subject>oxyhemoglobin</subject><subject>Oxyhemoglobins - chemistry</subject><subject>Oxyhemoglobins - metabolism</subject><subject>peroxidase</subject><subject>Peroxidase - metabolism</subject><subject>Postmortem Changes</subject><subject>protein aggregates</subject><subject>skeletal muscle</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>tilapia (common name)</subject><subject>Tilapia - blood</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U9v0zAYBnALgVg3OPAFIBeQOARe2_GfHKfCGGPSKtqdrTeuPVKSOLNTqf32GLVaL0icfHh_eu3nMSFvKHyiwOjnjYdKU1CbZ2RGBYNSUKqfkxnkYamFpGfkPKUNAGih4CU5o0ILXtFqRi4XMYwuTq1LRfDFqu1wbLGYY2zCbl8WOKyLu93-l-vDQxeadihwKhYhTX2Ik-uL8foVeeGxS-718bwg91dfV_Pr8vbu2_f55W2JFZdTfsa64jVnEqV3HpW2VoBmolGsdk0FXHpKmWe-ZrphHK2mjoNwXq-5bZjgF-TDYe8Yw-PWpcn0bbKu63BwYZuMVErznP6_kCpeSc15hh8P0MaQUnTejLHtMe4NBfO3WPNUbLZvj0u3Te_WJ3lsMoP3R4DJYucjDrZNJydVzl7r7MqDa9Pkdk9zjL9zAq6EWS2W5ubHz-XqC78xkP27g_cYDD7EvPN-yYByoFBBLenpZrTJbMI2Dvkb_hHhDx_eopo</recordid><startdate>20050504</startdate><enddate>20050504</enddate><creator>Kristinsson, Hordur G</creator><creator>Mony, Swapna S</creator><creator>Petty, Holly T</creator><general>American Chemical Society</general><scope>FBQ</scope><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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>20050504</creationdate><title>Properties of Tilapia Carboxy- and Oxyhemoglobin at Postmortem pH</title><author>Kristinsson, Hordur G ; Mony, Swapna S ; Petty, Holly T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a436t-85d439326a6fefa78cc50825b729eb4036f112f2f928b23ac81e305ef8d3cb253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>autoxidation</topic><topic>Biological and medical sciences</topic><topic>carbon monoxide</topic><topic>carboxyhemoglobin</topic><topic>Carboxyhemoglobin - chemistry</topic><topic>Carboxyhemoglobin - metabolism</topic><topic>Drug Stability</topic><topic>enzyme activity</topic><topic>Fish and seafood industries</topic><topic>fish fillets</topic><topic>Food industries</topic><topic>food processing</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hemoglobin</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Hydrogen-Ion Concentration</topic><topic>Oreochromis niloticus</topic><topic>oxyhemoglobin</topic><topic>Oxyhemoglobins - chemistry</topic><topic>Oxyhemoglobins - metabolism</topic><topic>peroxidase</topic><topic>Peroxidase - metabolism</topic><topic>Postmortem Changes</topic><topic>protein aggregates</topic><topic>skeletal muscle</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>tilapia (common name)</topic><topic>Tilapia - blood</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kristinsson, Hordur G</creatorcontrib><creatorcontrib>Mony, Swapna S</creatorcontrib><creatorcontrib>Petty, Holly T</creatorcontrib><collection>AGRIS</collection><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>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</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>Kristinsson, Hordur G</au><au>Mony, Swapna S</au><au>Petty, Holly T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Properties of Tilapia Carboxy- and Oxyhemoglobin at Postmortem pH</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2005-05-04</date><risdate>2005</risdate><volume>53</volume><issue>9</issue><spage>3643</spage><epage>3649</epage><pages>3643-3649</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Hemoglobin plays an important role in the color and oxidative stability of seafoods. A recent practice in the seafood industry is to stabilize muscle color by the application of gases containing carbon monoxide. The goal of this study was to examine and compare the properties of tilapia hemoglobin complexed to either O2 (Oxy-Hb) or CO (CO-Hb) at pH 6.5, which reflects the tilapia muscle postmortem pH. CO-Hb was significantly (p < 0.01) more stable against autoxidation compared to Oxy-Hb when kept at 4 and −30 °C for 23 days. Almost no loss of CO was detected for both temperatures according to the UV−vis spectra of Hb. This stabilization was also believed to play a role in increased protein structure stabilization (p < 0.001) since less protein aggregation was seen for CO-Hb. The higher protein stabilization for Hb was linked to the heme group, which was maintained in its reduced state longer for CO-Hb vs Oxy-Hb and was likely less exposed to solvent. CO-Hb had significantly (p < 0.01) less peroxidase activity than Oxy-Hb and thus reactivity with H2O2. The pro-oxidative activity of CO-Hb was significantly (p < 0.01) reduced in a linoleic acid micelle system compared to that of Oxy-Hb, while smaller differences in activity were seen in a washed cod and tilapia muscle model system. Keywords: Hemoglobin; tilapia; CO (carbon monoxide); O2 (oxygen); autoxidation; stability; peroxidase; pro-oxidative; lipid oxidation</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15853414</pmid><doi>10.1021/jf048107j</doi><tpages>7</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 2005-05, Vol.53 (9), p.3643-3649 |
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| source | MEDLINE; ACS_美国化学学会期刊（与NSTL共建） |
| subjects | Animals autoxidation Biological and medical sciences carbon monoxide carboxyhemoglobin Carboxyhemoglobin - chemistry Carboxyhemoglobin - metabolism Drug Stability enzyme activity Fish and seafood industries fish fillets Food industries food processing Fundamental and applied biological sciences. Psychology hemoglobin Hydrogen Peroxide - metabolism Hydrogen-Ion Concentration Oreochromis niloticus oxyhemoglobin Oxyhemoglobins - chemistry Oxyhemoglobins - metabolism peroxidase Peroxidase - metabolism Postmortem Changes protein aggregates skeletal muscle Spectrophotometry, Ultraviolet tilapia (common name) Tilapia - blood |
| title | Properties of Tilapia Carboxy- and Oxyhemoglobin at Postmortem pH |
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