Use of meat fluorescence emission as a marker of oxidation promoted by cooking.

Accumulation of fluorescent pigments in cooked bovine meat (M. Longissimus thoracis) was studied in relationship with the heating parameters (time and temperature). Muscles were aged at 4°C for 11days under vacuum before cooking. Meat cooking was performed by applying jets of steam. Three different heating treatments were tested: two with constant surface temperatures of 65 and 96°C for 300s, and one with a continuously increasing surface temperature up to 207°C. After extraction in water/dichloromethane/ethanol, fluorescence pigments were distributed between the apolar phase (emission 420-440nm after excitation at 360nm) and the polar phase, where two emission peaks were seen (emission 410-430 and 515nm after excitation at 360nm). Fluorescence in the two phases was little affected by heating at the two constant temperatures while it increased exponentially after 1min of treatment, as the varying temperature reached 141°C. The maximum fluorescence increases, measured in the extreme conditions of cooking (207°C/300s), were of 5000% in the apolar phase and 1700% in the polar phase. Thiobarbituric acid reactive substances (TBARS) and protein carbonyls were measured in parallel. The correlations between these two parameters and the fluorescence emission demonstrated that the interaction between proteins and aldehyde products of lipid peroxidation was mainly involved in the production of fluorescent pigments in cooked meat.

[1]  J Moan,et al.  Measurement of lipid oxidation and porphyrins in high oxygen modified atmosphere and vacuum-packed minced turkey and pork meat by fluorescence spectra and images. , 2006, Meat science.

[2]  T. Beveridge,et al.  Water sorption and crispness of fat-free apple chips , 2002 .

[3]  P. Gatellier,et al.  Antioxidant enzyme activities in beef in relation to oxidation of lipid and myoglobin. , 1996, Meat science.

[4]  S. W. Lin,et al.  Protein damage and degradation by oxygen radicals. II. Modification of amino acids. , 1987, The Journal of biological chemistry.

[5]  E. Decker,et al.  ALTERATIONS OF MUSCLE PROTEIN FUNCTIONALITY BY OXIDATIVE AND ANTIOXIDATIVE PROCESSES , 1995 .

[6]  V. Santé-Lhoutellier,et al.  Effect of meat cooking on physicochemical state and in vitro digestibility of myofibrillar proteins. , 2008, Journal of agricultural and food chemistry.

[7]  J. Richardson,et al.  Formation of reactive intermediates from Amadori compounds under physiological conditions. , 1995, Archives of biochemistry and biophysics.

[8]  P. Burcham,et al.  Introduction of carbonyl groups into proteins by the lipid peroxidation product, malondialdehyde. , 1996, Biochemical and biophysical research communications.

[9]  Y R Chen,et al.  Analysis of visible reflectance spectra of stored, cooked and diseased chicken meats. , 2001, Meat science.

[10]  M. Viau,et al.  Effect of dietary fat and vitamin E on colour stability and on lipid and protein oxidation in Turkey meat during storage. , 1998, Meat science.

[11]  E. Stadtman,et al.  Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction. , 1993, The Journal of biological chemistry.

[12]  K. Davies.  Protein damage and degradation by oxygen radicals. I. general aspects. , 1987, The Journal of biological chemistry.

[13]  Jens Petter Wold,et al.  Nondestructive Assessment of Lipid Oxidation in Minced Poultry Meat by Autofluorescence Spectroscopy , 2000 .

[14]  E. Stadtman,et al.  Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[15]  T. Labuza,et al.  Effect of green tea flavonoids on Maillard browning in UHT milk , 2007 .

[16]  C. Dillard,et al.  Fluorescent products from reaction of peroxidizing polyunsaturated fatty acids with phosphatidyl ethanolamine and phenylalanine , 1973, Lipids.

[17]  M. Morzel,et al.  Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins. , 2006, Meat science.

[18]  Š. Horvat,et al.  Study of degradation pathways of Amadori compounds obtained by glycation of opioid pentapeptide and related smaller fragments: stability, reactions, and spectroscopic properties. , 2003, Biopolymers.

[19]  D. Yin,et al.  Test-tube simulated lipofuscinogenesis. Effect of oxidative stress on autophagocytotic degradation , 1995, Mechanisms of Ageing and Development.

[20]  S. Portanguen,et al.  Prediction of surface and under surface temperatures on poultry muscles and poultry skins subjected to jets of superheated steam , 2008 .

[21]  J. Wold,et al.  Fluorescence in aldehyde model systems related to lipid oxidation , 2006 .

[22]  Harjinder Singh.  Modification of food proteins by covalent crosslinking , 1991 .

[23]  K. Yamauchi,et al.  A Lipid Peroxidation-derived Aldehyde, 4-Hydroxy-2-nonenal and ω6 Fatty Acids Contents in Meats , 1995 .

[24]  I. V. D. Plancken,et al.  Effect of heat-treatment on the physico-chemical properties of egg white proteins: A kinetic study , 2006 .

[25]  E. Stadtman,et al.  Age-related changes in oxidized proteins. , 1987, The Journal of biological chemistry.

[26]  A. Kulmyrzaev,et al.  Determination of lactulose and furosine in milk using front-face fluorescence spectroscopy , 2002 .

[27]  E. Stadtman,et al.  Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. , 1990, Free radical biology & medicine.

[28]  C. Berri,et al.  Use of a fluorescence front face technique for measurement of lipid oxidation during refrigerated storage of chicken meat. , 2007, Meat science.

[29]  Purificación García-Segovia,et al.  Effect of cooking method on mechanical properties, color and structure of beef muscle (M. pectoralis) , 2007 .

[30]  B. Friguet,et al.  Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease. , 1994, The Journal of biological chemistry.

[31]  B. Frei,et al.  Mechanisms of copper- and iron-dependent oxidative modification of human low density lipoprotein. , 1993, Journal of lipid research.

[32]  J. M. Lee,et al.  Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus. , 2005, Meat science.

[33]  V. Kagan.  Lipid Peroxidation In Biomembranes , 1988 .

[34]  H. Bachmann,et al.  Interaction between propionibacteria and starter / non-starter lactic acid bacteria in Swiss-type cheeses , 2002 .

[35]  R. Guillén-Sans,et al.  The thiobarbituric acid (TBA) reaction in foods: a review. , 1998, Critical reviews in food science and nutrition.

[36]  E. Stadtman,et al.  Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. , 1993, Annual review of biochemistry.

[37]  Juliet A. Gerrard,et al.  Protein–protein crosslinking in food: methods, consequences, applications , 2002 .

[38]  D. V. Byrne,et al.  Descriptive sensory profiling and physical/chemical analyses of warmed-over flavour in pork patties from carriers and non-carriers of the RN(-) allele. , 2003, Meat science.

[39]  F. B. Whitfield,et al.  Changes in the composition of the fatty acids and aldehydes of meat lipids after heating , 2007 .

[40]  H. Buttkus.  The Reaction of Myosin with Malonaldehyde , 1967 .

[41]  V. Santé-Lhoutellier,et al.  Characterisation of fluorescent Schiff bases formed during oxidation of pig myofibrils. , 2007, Meat science.

[42]  D. V. Byrne,et al.  Sensory and chemical analysis of cooked porcine meat patties in relation to warmed-over flavour and pre-slaughter stress. , 2001, Meat science.

[43]  V. Santé-Lhoutellier,et al.  Technical note: A simplified procedure for myofibril hydrophobicity determination. , 2006, Meat science.

[44]  K. Davies,et al.  Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. , 2004, The international journal of biochemistry & cell biology.

[45]  D. V. Byrne,et al.  Sensory panel consistency during development of a vocabulary for warmed-over flavour , 2001 .

[46]  D. Pearce,et al.  You say lipofuscin, we say ceroid: Defining autofluorescent storage material , 2006, Neurobiology of Aging.

[47]  J. Harding,et al.  The reaction of malondialdehyde with lens proteins and the protective effect of aspirin. , 1993, Biochimica et biophysica acta.

[48]  V. Santé-Lhoutellier,et al.  Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins. , 2007, Journal of agricultural and food chemistry.

[49]  E. Tornberg,et al.  Effects of heat on meat proteins - Implications on structure and quality of meat products. , 2005, Meat science.

[50]  J. Baynes,et al.  Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. , 1995, Biochemistry.

[51]  F. Monahan,et al.  Measurement of lipid oxidation in meat and meat products , 1992 .