dc.creatorMøller, Jens K. S.
dc.creatorSkibsted, Leif H.
dc.date2006-12-01
dc.date2015-12-03T13:30:37Z
dc.date2015-12-03T13:30:37Z
dc.date.accessioned2018-03-29T01:24:41Z
dc.date.available2018-03-29T01:24:41Z
dc.identifierQuímica Nova. Sociedade Brasileira de Química, v. 29, n. 6, p. 1270-1278, 2006.
dc.identifier0100-4042
dc.identifierS0100-40422006000600024
dc.identifier10.1590/S0100-40422006000600024
dc.identifierhttp://dx.doi.org/10.1590/S0100-40422006000600024
dc.identifierhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422006000600024
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/23730
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/202423
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1302656
dc.descriptionAerobic 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.
dc.description1270
dc.description1278
dc.languageen
dc.publisherSociedade Brasileira de Química
dc.relationQuímica Nova
dc.rightsaberto
dc.sourceSciELO
dc.subjectmyoglobin complexes
dc.subjectheme iron
dc.subjectoxidative processes
dc.titleMyoglobins: the link between discoloration and lipid oxidation in muscle and meat
dc.typeArtículos de revistas


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