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Volumn 172, Issue , 2015, Pages 447-455

Protein modifications in cooked pork products investigated by a proteomic approach

Author keywords

Cooked hams; Emulsion sausages; Heat treatments; Muscle protein oxidation; Proteomics

Indexed keywords

AMINO ACIDS; CHAINS; ELECTROPHORESIS; EMULSIFICATION; HEAT TREATMENT; MASS SPECTROMETRY; MOLECULAR BIOLOGY; PROTEINS; SULFUR COMPOUNDS;

EID: 84907480717     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2014.09.099     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 33646529665 scopus 로고    scopus 로고
    • Meat cooking shrinkage: Measurement of a new meat quality parameter
    • S. Barbera, and S. Tassone Meat cooking shrinkage: Measurement of a new meat quality parameter Meat Science 73 2006 467 474
    • (2006) Meat Science , vol.73 , pp. 467-474
    • Barbera, S.1    Tassone, S.2
  • 2
    • 52249115647 scopus 로고    scopus 로고
    • The behaviour of the protein complex throughout the technological process in the production of cooked cold meats
    • G. Barbieri, and P. Rivaldi The behaviour of the protein complex throughout the technological process in the production of cooked cold meats Meat Science 80 2008 1132 1137
    • (2008) Meat Science , vol.80 , pp. 1132-1137
    • Barbieri, G.1    Rivaldi, P.2
  • 3
    • 84876317362 scopus 로고    scopus 로고
    • Survey of the chemical, physical, and sensory characteristics of currently produced mortadella bologna
    • G. Barbieri, M. Bergamaschi, Ge. Barbieri, and M. Franceschini Survey of the chemical, physical, and sensory characteristics of currently produced mortadella bologna Meat Science 94 2013 336 340
    • (2013) Meat Science , vol.94 , pp. 336-340
    • Barbieri, G.1    Bergamaschi, M.2    Barbieri Ge.3    Franceschini, M.4
  • 4
    • 22144489165 scopus 로고    scopus 로고
    • The use of proteomics in meat science
    • Review
    • E. Bendixen The use of proteomics in meat science Meat Science 71 2005 138 149 Review
    • (2005) Meat Science , vol.71 , pp. 138-149
    • Bendixen, E.1
  • 6
    • 33847141111 scopus 로고    scopus 로고
    • Characterisation of fluorescent Schiff bases formed during oxidation of pig myofibrils
    • I. Chelh, P. Gatellier, and V. Santé-Lhoutellier Characterisation of fluorescent Schiff bases formed during oxidation of pig myofibrils Meat Science 76 2007 210 215
    • (2007) Meat Science , vol.76 , pp. 210-215
    • Chelh, I.1    Gatellier, P.2    Santé-Lhoutellier, V.3
  • 7
    • 84985052489 scopus 로고
    • Heat-induced changes in myofibrillar proteins of bovine longissimus muscle
    • C.S. Cheng, and F.C. Parrish Jr. Heat-induced changes in myofibrillar proteins of bovine longissimus muscle Journal of Food Science 44 1979 22 24
    • (1979) Journal of Food Science , vol.44 , pp. 22-24
    • Cheng, C.S.1    Parrish, F.C.2
  • 9
    • 21144470425 scopus 로고
    • Differentiation of animal species by meat proteins. I. Detection of beef mixed with pork meat by isoelectric focusing of the A2 myosin light chain
    • A. Di Luccia, A. Santoro, A. Anastasio, T. Sarli, F. Manniti, and G. Boffa Differentiation of animal species by meat proteins. I. Detection of beef mixed with pork meat by isoelectric focusing of the A2 myosin light chain Italian Journal of Food Science 3 1992 195 204
    • (1992) Italian Journal of Food Science , vol.3 , pp. 195-204
    • Di Luccia, A.1    Santoro, A.2    Anastasio, A.3    Sarli, T.4    Manniti, F.5    Boffa, G.6
  • 10
    • 11444259281 scopus 로고    scopus 로고
    • Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams
    • A. Di Luccia, G. Picariello, G. Cacace, A. Scaloni, M. Faccia, and V. Liuzzi Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams Meat Science 69 2005 479 491
    • (2005) Meat Science , vol.69 , pp. 479-491
    • Di Luccia, A.1    Picariello, G.2    Cacace, G.3    Scaloni, A.4    Faccia, M.5    Liuzzi, V.6
  • 11
    • 84986532540 scopus 로고
    • Differential scanning calorimetry can determine kinetics of thermal denaturation of beef muscle proteins
    • C.J. Findlay, K.L. Parkin, and D.W. Stanley Differential scanning calorimetry can determine kinetics of thermal denaturation of beef muscle proteins Journal of Food Biochemistry 10 1989 1 15
    • (1989) Journal of Food Biochemistry , vol.10 , pp. 1-15
    • Findlay, C.J.1    Parkin, K.L.2    Stanley, D.W.3
  • 12
    • 0000524070 scopus 로고
    • Cooking effects on titin in fresh and processed beef products
    • J.D. Fritz, L.J. Dietrich, and M.L. Greaser Cooking effects on titin in fresh and processed beef products Journal of Muscle Foods 3 1992 133 140
    • (1992) Journal of Muscle Foods , vol.3 , pp. 133-140
    • Fritz, J.D.1    Dietrich, L.J.2    Greaser, M.L.3
  • 13
    • 0001679509 scopus 로고
    • Lipid hydroperoxide reactivity with proteins and amino acids: A review
    • H.W. Gardner Lipid hydroperoxide reactivity with proteins and amino acids: A review Journal of Agricultural and Food Chemistry 27 1979 220 229
    • (1979) Journal of Agricultural and Food Chemistry , vol.27 , pp. 220-229
    • Gardner, H.W.1
  • 14
    • 70249127867 scopus 로고    scopus 로고
    • Use of meat fluorescence emission as a marker of oxidation promoted by cooking
    • P. Gatellier, V. Santé-Lhoutellier, S. Portanguen, and A. Kondjoyan Use of meat fluorescence emission as a marker of oxidation promoted by cooking Meat Science 83 2009 651 656
    • (2009) Meat Science , vol.83 , pp. 651-656
    • Gatellier, P.1    Santé-Lhoutellier, V.2    Portanguen, S.3    Kondjoyan, A.4
  • 15
    • 0036980061 scopus 로고    scopus 로고
    • Protein-protein crosslinking in food: Methods, consequences, applications
    • J.A. Gerrard Protein-protein crosslinking in food: Methods, consequences, applications Trends in Food Science & Technology 13 2002 391 399
    • (2002) Trends in Food Science & Technology , vol.13 , pp. 391-399
    • Gerrard, J.A.1
  • 16
    • 0029257253 scopus 로고
    • 2-generated myoglobin radical in cross-linking of myosin
    • 2-generated myoglobin radical in cross-linking of myosin Free Radical Research 22 1995 215 227
    • (1995) Free Radical Research , vol.22 , pp. 215-227
    • Hanan, T.1    Shaklai, N.2
  • 17
    • 0012370381 scopus 로고
    • Factors affecting tenderness during heating of meat
    • C.O. Chichester, E.M. Mrak, G.F. Stewart, Academic Press New York
    • E. Laakkonen Factors affecting tenderness during heating of meat C.O. Chichester, E.M. Mrak, G.F. Stewart, Advances in food research Vol. 20 1973 Academic Press New York 257 323
    • (1973) Advances in Food Research , vol.20 , pp. 257-323
    • Laakkonen, E.1
  • 20
    • 0011480210 scopus 로고
    • The role of gap filaments in muscle and in meat
    • R.H. Locker The role of gap filaments in muscle and in meat Food Microstructure 3 1984 17 32
    • (1984) Food Microstructure , vol.3 , pp. 17-32
    • Locker, R.H.1
  • 21
    • 41149156956 scopus 로고    scopus 로고
    • Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links
    • M.N. Lund, C. Luxford, L.H. Skibsted, and M.J. Davies Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links Biochemical Journal 410 2008 565 574
    • (2008) Biochemical Journal , vol.410 , pp. 565-574
    • Lund, M.N.1    Luxford, C.2    Skibsted, L.H.3    Davies, M.J.4
  • 24
    • 0032142737 scopus 로고    scopus 로고
    • Flavour formation in meat and meat products: A review
    • D.S. Mottram Flavour formation in meat and meat products: A review Food Chemistry 62 1998 415 424
    • (1998) Food Chemistry , vol.62 , pp. 415-424
    • Mottram, D.S.1
  • 25
    • 0033481199 scopus 로고    scopus 로고
    • Changes in texture, cooking losses, and myofibrillar structure of bovine M. Semitendinosus during heating
    • K. Palka, and H. Daun Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosus during heating Meat Science 51 1999 237 243
    • (1999) Meat Science , vol.51 , pp. 237-243
    • Palka, K.1    Daun, H.2
  • 26
    • 84864288909 scopus 로고    scopus 로고
    • Molecular basis of intramolecular electron transfer in proteins during radical-mediated oxidations: Computer simulation studies in model tyrosine-cysteine peptides in solution
    • A.A. Petruk, S. Bartesaghi, M. Trujillo, D.A. Estrin, D. Murgida, and B. Kalyanaraman Molecular basis of intramolecular electron transfer in proteins during radical-mediated oxidations: Computer simulation studies in model tyrosine-cysteine peptides in solution Archives of Biochemistry and Biophysics 525 1 2012 82 91
    • (2012) Archives of Biochemistry and Biophysics , vol.525 , Issue.1 , pp. 82-91
    • Petruk, A.A.1    Bartesaghi, S.2    Trujillo, M.3    Estrin, D.A.4    Murgida, D.5    Kalyanaraman, B.6
  • 28
    • 79959241187 scopus 로고    scopus 로고
    • Proteomic analysis of pork meat in the production of cooked ham
    • B. Pioselli, G. Paredi, and A. Mozzarelli Proteomic analysis of pork meat in the production of cooked ham Molecular BioSystems 7 2011 2252 2260
    • (2011) Molecular BioSystems , vol.7 , pp. 2252-2260
    • Pioselli, B.1    Paredi, G.2    Mozzarelli, A.3
  • 31
    • 38249024098 scopus 로고
    • Electron microscopy of bovine muscles: II - The effects of heat denaturation on post rigor sarcolemma and endomysium
    • R.W.D. Rowe Electron microscopy of bovine muscles: II - The effects of heat denaturation on post rigor sarcolemma and endomysium Meat Science 26 1989 281 294
    • (1989) Meat Science , vol.26 , pp. 281-294
    • Rowe, R.W.D.1
  • 34
    • 0000913319 scopus 로고
    • Use of sonication and size exclusion performance liquid chromatography in the study of wheat flour proteins. I. Dissolution of total proteins in the absence of reducing agents
    • N.K. Singh, G.R. Donovan, I.L. Batey, and F. MacRitchie Use of sonication and size exclusion performance liquid chromatography in the study of wheat flour proteins. I. Dissolution of total proteins in the absence of reducing agents Cereal Chemistry 67 2 1990 150 161
    • (1990) Cereal Chemistry , vol.67 , Issue.2 , pp. 150-161
    • Singh, N.K.1    Donovan, G.R.2    Batey, I.L.3    Macritchie, F.4
  • 35
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Opening Review Article
    • E.R. Stadtman, and R.L. Levine Free radical-mediated oxidation of free amino acids and amino acid residues in proteins Amino Acids 25 2003 207 218 Opening Review Article
    • (2003) Amino Acids , vol.25 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 36
    • 79959979853 scopus 로고    scopus 로고
    • Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility
    • W. Sun, F. Zhou, M. Zhao, B. Yang, and C. Cui Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility Food Chemistry 129 2011 472 478
    • (2011) Food Chemistry , vol.129 , pp. 472-478
    • Sun, W.1    Zhou, F.2    Zhao, M.3    Yang, B.4    Cui, C.5
  • 37
    • 33644522736 scopus 로고    scopus 로고
    • Effects of heat on meat proteins: Implications on structure and quality of meat products
    • Review
    • E. Tornberg Effects of heat on meat proteins: Implications on structure and quality of meat products Meat Science 70 2005 493 508 Review
    • (2005) Meat Science , vol.70 , pp. 493-508
    • Tornberg, E.1
  • 39
    • 0347991814 scopus 로고    scopus 로고
    • Histidine and lysine as targets of oxidative modification
    • Review Article
    • K. Uchida Histidine and lysine as targets of oxidative modification Amino Acids 25 2003 249 257 Review Article
    • (2003) Amino Acids , vol.25 , pp. 249-257
    • Uchida, K.1
  • 40
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • W. Vogt Oxidation of methionyl residues in proteins: Tools, targets, and reversal Free Radical Biology and Medicine 18 1995 93 105
    • (1995) Free Radical Biology and Medicine , vol.18 , pp. 93-105
    • Vogt, W.1


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