Myoglobins: the link between discoloration and lipid oxidation in muscle and meat
Autor(a) principal: | |
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Data de Publicação: | 2006 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Química Nova (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422006000600024 |
Resumo: | Aerobic metabolism changes rapidly to glycolysis post-mortem resulting in a pH-decrease during the transformation of muscle in to meat affecting ligand binding and redox potential of the heme iron in myoglobin, the meat pigment. The "inorganic chemistry" of meat involves (i) redox-cycling between iron(II), iron(III), and iron(IV)/protein radicals; (ii) ligand exchange processes; and (iii) spin-equilibra with a change in coordination number for the heme iron. In addition to the function of myoglobin for oxygen storage, new physiological roles of myoglobin are currently being discovered, which notably find close parallels in the processes in fresh meat and nitrite-cured meat products. Myoglobin may be characterized as a bioreactor for small molecules like O2, NO, CO, CO2, H2O, and HNO with importance in bio-regulation and in protection against oxidative stress in vivo otherwise affecting lipids in membranes. Many of these processes may be recognised as colour changes in fresh meat and cured meat products under different atmospheric conditions, and could also be instructive for teaching purposes. |
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Myoglobins: the link between discoloration and lipid oxidation in muscle and meatmyoglobin complexesheme ironoxidative processesAerobic metabolism changes rapidly to glycolysis post-mortem resulting in a pH-decrease during the transformation of muscle in to meat affecting ligand binding and redox potential of the heme iron in myoglobin, the meat pigment. The "inorganic chemistry" of meat involves (i) redox-cycling between iron(II), iron(III), and iron(IV)/protein radicals; (ii) ligand exchange processes; and (iii) spin-equilibra with a change in coordination number for the heme iron. In addition to the function of myoglobin for oxygen storage, new physiological roles of myoglobin are currently being discovered, which notably find close parallels in the processes in fresh meat and nitrite-cured meat products. Myoglobin may be characterized as a bioreactor for small molecules like O2, NO, CO, CO2, H2O, and HNO with importance in bio-regulation and in protection against oxidative stress in vivo otherwise affecting lipids in membranes. Many of these processes may be recognised as colour changes in fresh meat and cured meat products under different atmospheric conditions, and could also be instructive for teaching purposes.Sociedade Brasileira de Química2006-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422006000600024Química Nova v.29 n.6 2006reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0100-40422006000600024info:eu-repo/semantics/openAccessMøller,Jens K. S.Skibsted,Leif H.eng2011-09-06T00:00:00Zoai:scielo:S0100-40422006000600024Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2011-09-06T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat |
title |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat |
spellingShingle |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat Møller,Jens K. S. myoglobin complexes heme iron oxidative processes |
title_short |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat |
title_full |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat |
title_fullStr |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat |
title_full_unstemmed |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat |
title_sort |
Myoglobins: the link between discoloration and lipid oxidation in muscle and meat |
author |
Møller,Jens K. S. |
author_facet |
Møller,Jens K. S. Skibsted,Leif H. |
author_role |
author |
author2 |
Skibsted,Leif H. |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Møller,Jens K. S. Skibsted,Leif H. |
dc.subject.por.fl_str_mv |
myoglobin complexes heme iron oxidative processes |
topic |
myoglobin complexes heme iron oxidative processes |
description |
Aerobic metabolism changes rapidly to glycolysis post-mortem resulting in a pH-decrease during the transformation of muscle in to meat affecting ligand binding and redox potential of the heme iron in myoglobin, the meat pigment. The "inorganic chemistry" of meat involves (i) redox-cycling between iron(II), iron(III), and iron(IV)/protein radicals; (ii) ligand exchange processes; and (iii) spin-equilibra with a change in coordination number for the heme iron. In addition to the function of myoglobin for oxygen storage, new physiological roles of myoglobin are currently being discovered, which notably find close parallels in the processes in fresh meat and nitrite-cured meat products. Myoglobin may be characterized as a bioreactor for small molecules like O2, NO, CO, CO2, H2O, and HNO with importance in bio-regulation and in protection against oxidative stress in vivo otherwise affecting lipids in membranes. Many of these processes may be recognised as colour changes in fresh meat and cured meat products under different atmospheric conditions, and could also be instructive for teaching purposes. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422006000600024 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422006000600024 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0100-40422006000600024 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Química Nova v.29 n.6 2006 reponame:Química Nova (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Química Nova (Online) |
collection |
Química Nova (Online) |
repository.name.fl_str_mv |
Química Nova (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
quimicanova@sbq.org.br |
_version_ |
1750318105739919360 |