Cooking-Induced Protein Modifications in Meat

Comprehensive Reviews in Food Science and Food Safety

Volumn 16, Issue 1, 2017, Pages 141-159

  Yu, Tzer Yang ^a,b   Morton, James D ^b,d   Clerens, Stefan ^a,d   Dyer, Jolon M ^a,b,c,d  

^a AGRESEARCH LTD   (New Zealand)

^b LINCOLN UNIVERSITY   (New Zealand)

^c MASSEY UNIVERSITY   (New Zealand)

^d UNIVERSITY OF CANTERBURY   (New Zealand)

Author keywords

cooking; heating; meat; protein aggregation; protein modifications

Indexed keywords

AMINO ACIDS; CARBONYLATION; COOKING; HEAT TREATMENT; HEATING; MAMMALS; MEATS;

AMINO ACID RESIDUES; AROMATIC RESIDUES; MAILLARD REACTION PRODUCTS; NUTRITIONAL AND FUNCTIONAL PROPERTIES; PRIMARY STRUCTURES; PROTEIN AGGREGATION; PROTEIN CARBONYLATION; PROTEIN MODIFICATIONS;

PROTEINS;

EID: 85005993310     PISSN: None     EISSN: 15414337     Source Type: Journal    
DOI: 10.1111/1541-4337.12243     Document Type: Article

References (187)

1. Addis MF, Tanca A, Pagnozzi D, Crobu S, Fanciulli G, Cossu-Rocca P, Uzzau S. 2009a. Generation of high-quality protein extracts from formalin-fixed, paraffin-embedded tissues. Proteomics 9:3815–23.
2. Addis MF, Tanca A, Pagnozzi D, Rocca S, Uzzau S. 2009b. 2-D PAGE and MS analysis of proteins from formalin-fixed, paraffin-embedded tissues. Proteomics 9:4329–39.
3. An H, Marshall MR, Otwell WS, Wei CI. 1988. Electrophoretic identification of raw and cooked shrimp using various protein extraction systems. J Food Sci 53:313–8.
4. Apostolovic D, Tran TAT, Hamsten C, Starkhammar M, Cirkovic Velickovic T, van Hage M. 2014. Immunoproteomics of processed beef proteins reveal novel galactose-α-1,3-galactose-containing allergens. Allergy 69:1308–15.
5. Arena S, Salzano AM, Renzone G, D'Ambrosio C, Scaloni A. 2014. Non-enzymatic glycation and glycoxidation protein products in foods and diseases: an interconnected, complex scenario fully open to innovative proteomic studies. Mass Spectrometry Rev 33:49–77.
6. Astruc T. 2014. Carcass composition, muscle structure, and contraction. In: Dikeman M, Devine C, editors. Encyclopedia of meat sciences. 2nd ed. Oxford: Academic Press. p 148–66.
7. Astruc T, Gatellier P, Labas R, Lhoutellier VS, Marinova P. 2010. Microstructural changes in m. rectus abdominis bovine muscle after heating. Meat Sci 85:743–51.
8. Augustyniak E, Adam A, Wojdyla K, Rogowska-Wrzesinska A, Willetts R, Korkmaz A, Atalay M, Weber D, Grune T, Borsa C, Gradinaru D, Chand Bollineni R, Fedorova M, Griffiths HR. 2015. Validation of protein carbonyl measurement: a multi-centre study. Redox Biol 4:149–57.
9. Bao Y, Ertbjerg P. 2015. Relationship between oxygen concentration, shear force and protein oxidation in modified atmosphere packaged pork. Meat Sci 110:174–9.
10. Barbieri G, Rivaldi P. 2008. The behaviour of the protein complex throughout the technological process in the production of cooked cold meats. Meat Sci 80:1132–7.
11. Bax ML, Aubry L, Ferreira C, Daudin JD, Gatellier P, Rémond D, Santé-Lhoutellier V. 2012. Cooking temperature is a key determinant of in vitro meat protein digestion rate: investigation of underlying mechanisms. J Agric Food Chem 60:2569–76.
12. Bax M-L, Buffière C, Hafnaoui N, Gaudichon C, Savary-Auzeloux I, Dardevet D, Santé-Lhoutellier V, Rémond D. 2013a. Effects of meat cooking, and of ingested amount, on protein digestion speed and entry of residual proteins into the colon: a study in minipigs. PLoS ONE 8:e61252.
13. Bax ML, Sayd T, Aubry L, Ferreira C, Viala D, Chambon C, Rémond D, Santé-Lhoutellier V. 2013b. Muscle composition slightly affects in vitro digestion of aged and cooked meat: identification of associated proteomic markers. Food Chem 136:1249–62.
14. Bechtel PJ. 1986. Muscle development and contractile proteins. In: Bechtel PJ, editor. Muscle as food. Orlando, Fla.: Academic Press. p 1–35.
15. Bejerholm C, Tørngren MA, Aaslyng MD. 2014. Cooking of meat—cooking of meat. In: Dikeman M, Devine C, editors. Encyclopedia of meat sciences. 2nd ed. Oxford: Academic Press. p 370–6.
16. Bendall JR, Restall DJ. 1983. The cooking of single myofibres, small myofibre bundles and muscle strips from beef M. psoas and M. sternomandibularis muscles at varying heating rates and temperatures. Meat Sci 8:93–117.
17. Beuk JF, Chornock FW, Rice EE. 1949. The effect of heat on the availability of pork protein in vivo and in vitro. J Biol Chem 180:1243–51.
18. Bjarnadóttir SG, Hollung K, Høy M, Bendixen E, Codrea MC, Veiseth-Kent E. 2012. Changes in protein abundance between tender and tough meat from bovine longissimus thoracis muscle assessed by isobaric tag for relative and absolute quantitation (iTRAQ) and 2-dimensional gel electrophoresis analysis. J Anim Sci 90:2035–43.
19. Bodwell CE, McClain PE. 1971. Chemistry of animal tissues. In: Price JF, Schweigert BS, editors. The science of meat and meat products. 2nd ed. San Francisco, Calif.: W. H. Freeman. p 78–207.
20. Bouley J, Chambon C, Picard B. 2004. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 4:1811–24.
21. Bruneel C, Pareyt B, Brijs K, Delcour JA. 2010. The impact of the protein network on the pasting and cooking properties of dry pasta products. Food Chem 120:371–8.
22. Cai W, Ramdas M, Zhu L, Chen X, Striker GE, Vlassara H. 2012. Oral advanced glycation endproducts (AGEs) promote insulin resistance and diabetes by depleting the antioxidant defenses AGE receptor-1 and sirtuin 1. Proc Natl Acad Sci USA 109:15888–93.
23. Campbell KP, Stull JT. 2003. Skeletal muscle basement membrane-sarcolemma-cytoskeleton interaction minireview series. J Biol Chem 278:12599–600.
24. Cassens RG. 1971. Microscopic structure of animal tissues. In: Price JF, Schweigert BS, editors. The science of meat and meat products. 2nd ed. San Francisco, Calif.: W. H. Freeman. p 11–77.
25. Chaze T, Bouley J, Chambon C, Barboiron C, Picard B. 2006. Mapping of alkaline proteins in bovine skeletal muscle. Proteomics 6:2571–5.
26. Chen G, Smith SJ. 2015. Determination of advanced glycation end products in cooked meat products. Food Chem 168:190–5.
27. Chen L, Ma L, Zhou M, Liu Y, Zhang Y. 2014. Effects of pressure on gelatinization of collagen and properties of extracted gelatins. Food Hydrocolloids 36:316–22.
28. Cheng C-S, Parrish FC. 1979. Heat-induced changes in, myofibrillar proteins of bovine longissimus muscle. J Food Sci 44:22–4.
29. Chepanoske CL, Brown K, Turteltaub KW, Dingley KH. 2004. Characterization of a peptide adduct formed by N-acetoxy-2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP), a reactive intermediate of the food carcinogen PhIP. Food Chem Toxicol 42:1367–72.
30. Christensen M, Purslow PP, Larsen LM. 2000. The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue. Meat Sci 55:301–7.
31. Christensen M, Ertbjerg P, Failla S, Sañudo C, Richardson RI, Nute GR, Olleta JL, Panea B, Albertí P, Juárez M, Hocquette J-F, Williams JL. 2011. Relationship between collagen characteristics, lipid content and raw and cooked texture of meat from young bulls of fifteen European breeds. Meat Sci 87:61–5.
32. Claeys WL, Verraes C, Cardoen S, De Block J, Huyghebaert A, Raes K, Dewettinck K, Herman L. 2014. Consumption of raw or heated milk from different species: an evaluation of the nutritional and potential health benefits. Food Control 42:188–201.
33. Clark KA, McElhinny AS, Beckerle MC, Gregorio CC. 2002. Striated muscle cytoarchitecture: an intricate web of form and function. Annu Rev Cell Development Biol 18:637–706.
34. Clerens S, Plowman JE, Dyer JM. 2012. Food proteomics: mapping modifications. In: Heazlewood J, Petzold CJ, editors. Proteomic applications in biology. Croatia, Rijeka: InTech. p 3–32.
35. Cui C, Zhou X, Zhao M, Yang B. 2009. Effect of thermal treatment on the enzymatic hydrolysis of chicken proteins. Innov Food Sci Emerg Technol 10:37–41.
36. Dai Y, Miao J, Yuan S-Z, Liu Y, Li X-M, Dai R-T. 2013. Colour and sarcoplasmic protein evaluation of pork following water bath and ohmic cooking. Meat Sci 93:898–905.
37. Dai Y, Zhang Q-N, Wang L, Liu Y, Li X-M, Dai R-T. 2014. Changes in shear parameters, protein degradation and ultrastructure of pork following water bath and ohmic cooking. Food Bioprocess Technol 7:1393–403.
38. Daniel H. 2004. Molecular and integrative physiology of intestinal peptide transport. Annu Rev Physiol 66:361–84.
39. Davey CL, Winger RJ. 1988. Muscle to meat (biochemical aspects) In: Cross HR, Overby AJ, editors. World animal science. Vol. B3, Meat science, milk science and technology. London: Elsevier Science Publishers. p 3–31.
40. Davis PJ, Williams SC. 1998. Protein modification by thermal processing. Allergy 53:102–5.
41. Deb-Choudhury S, Haines S, Harland D, Clerens S, van Koten C, Dyer J. 2014. Effect of cooking on meat proteins: mapping hydrothermal protein modification as a potential indicator of bioavailability. J Agric Food Chem 62:8187–96.
42. Decker EA, Park Y. 2010. Healthier meat products as functional foods. Meat Sci 86:49–55.
43. Deshmukh AS, Murgia M, Nagaraj N, Treebak JT, Cox J, Mann M. 2015. Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways, and transcription factors. Mol Cell Proteomics 14:841–53.
44. Devine CE. 2014. Conversion of muscle to meat—aging. In: Dikeman M, Devine C, editors. Encyclopedia of meat sciences. 2nd ed. Oxford: Academic Press. p 329–38.
45. Di Luca A, Elia G, Hamill R, Mullen AM. 2013. 2D DIGE proteomic analysis of early post mortem muscle exudate highlights the importance of the stress response for improved water-holding capacity of fresh pork meat. Proteomics 13:1528–44.
46. Di Luccia A, la Gatta B, Nicastro A, Petrella G, Lamacchia C, Picariello G. 2015. Protein modifications in cooked pork products investigated by a proteomic approach. Food Chem 172:447–55.
47. Dingley KH, Freeman SPHT, Nelson DO, Garner RC, Turteltaub KW. 1998. Covalent binding of 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline to albumin and hemoglobin at environmentally relevant doses: comparison of human subjects and f344 rats. Drug Metabol Dispos 26:825–8.
48. Dyer JM, Bringans SD, Bryson WG. 2006. Characterisation of photo-oxidation products within photoyellowed wool proteins: tryptophan and tyrosine derived chromophores. Photochem Photobiol Sci 5:698–706.
49. Dyer JM, Plowman JE, Krsinic GL, Deb-Choudhury S, Koehn H, Millington KR, Clerens S. 2010. Proteomic evaluation and location of UVB-induced photo-oxidation in wool. J Photochem Photobiol B: Biol 98:118–27.
50. Estévez M. 2011. Protein carbonyls in meat systems: a review. Meat Sci 89:259–79.
51. Estévez M, Luna C. 2016. Dietary protein oxidation: a silent threat to human health? Crit Rev Food Sci Nutr doi: 10.1080/10408398.2016.1165182. in press.
52. Farouk MM, Wu G, Frost DA, Clerens S, Knowles SO. 2014. The in vitro digestibility of beef varies with its inherent ultimate pH. Food Funct 5:2759–67.
53. Feng X, Li C, Ullah N, Hackman RM, Chen L, Zhou G. 2015. Potential biomarker of myofibrillar protein oxidation in raw and cooked ham: 3-nitrotyrosine formed by nitrosation. J Agric Food Chem 63:10957–64.
54. Fernández García A, Butz P, Trierweiler B, Zöller H, Stärke J, Pfaff E, Tauscher B. 2003. Pressure/temperature combined treatments of precursors yield hormone-like peptides with pyroglutamate at the N terminus. J Agric Food Chem 51:8093–7.
55. Filgueras RS, Gatellier P, Ferreira C, Zambiazi RC, Santé-Lhoutellier V. 2011. Nutritional value and digestion rate of rhea meat proteins in association with storage and cooking processes. Meat Sci 89:6–12.
56. Fraenkel-Conrat H, Cooper M. 1944. The use of dyes for the determination of acid and basic groups in proteins. J Biol Chem 154:239–46.
57. Ganhão R, Morcuende D, Estévez M. 2010. Tryptophan depletion and formation of α-aminoadipic and γ-glutamic semialdehydes in porcine burger patties with added phenolic-rich fruit extracts. J Agric Food Chem 58:3541–8.
58. García-Segovia P, Andrés-Bello A, Martínez-Monzó J. 2007. Effect of cooking method on mechanical properties, color and structure of beef muscle (m. pectoralis). J Food Engr 80:813–21.
59. Gatellier P, Kondjoyan A, Portanguen S, Grève E, Yoon K, Santé-Lhoutellier V. 2009a. Determination of aromatic amino acid content in cooked meat by derivative spectrophotometry: implications for nutritional quality of meat. Food Chem 114:1074–8.
60. Gatellier P, Santé-Lhoutellier V, Portanguen S, Kondjoyan A. 2009b. Use of meat fluorescence emission as a marker of oxidation promoted by cooking. Meat Sci 83:651–6.
61. Gatellier P, Kondjoyan A, Portanguen S, Santé-Lhoutellier V. 2010. Effect of cooking on protein oxidation in n-3 polyunsaturated fatty acids-enriched beef. Implication on nutritional quality. Meat Sci 85:645–50.
62. Gibis M. 2016. Heterocyclic aromatic amines in cooked meat products: causes, formation, occurrence, and risk assessment. Comp Rev Food Sci Food Safety 15:269–302.
63. Goll DE, Kleese WC, Szpacenko A. 1989. Skeletal muscle proteases and protein turnover. In: Campion DR, Hausman GJ, Martin RJ, editors. Animal growth regulation. New York, N.Y.: Plenum Press. p 141–82.
64. Goll DE, Neti G, Mares SW, Thompson VF. 2008. Myofibrillar protein turnover: the proteasome and the calpains. J Anim Sci 86:E19–35.
65. Greenwood DA, Kraybill HR, Schweigert BS. 1951. Amino acid composition of fresh and cooked beef cuts. J Biol Chem 193:23–8.
66. Grosvenor AJ, Morton JD, Dyer JM. 2011. Proteomic characterisation of hydrothermal redox damage. J Sci Food Agric 91:2806–13.
67. Hakimov HA, Walters S, Wright TC, Meidinger RG, Verschoor CP, Gadish M, Chiu DKY, Strömvik MV, Forsberg CW, Golovan SP. 2009. Application of iTRAQ to catalogue the skeletal muscle proteome in pigs and assessment of effects of gender and diet dephytinization. Proteomics 9:4000–16.
68. Hamm R, Deatherage FE. 1960. Changes in hydration, solubility and charges of muscle proteins during heating of meat. J Food Sci 25:587–610.
69. Hebling CM, McFarland MA, Callahan JH, Ross MM. 2013. Global proteomic screening of protein allergens and advanced glycation endproducts in thermally processed peanuts. J Agric Food Chem 61:5638–48.
70. Hernández-López SH, Rodríguez-Carpena JG, Lemus-Flores C, Galindo-García J, Estévez M. 2016. Antioxidant protection of proteins and lipids in processed pork loin chops through feed supplementation with avocado. J Food Sci Technol 53:2788–96.
71. Hill F. 1966. The solubility of intramuscular collagen in meat animals of various ages. J Food Sci 31:161–6.
72. Højlund K, Yi Z, Hwang H, Bowen B, Lefort N, Flynn CR, Langlais P, Weintraub ST, Mandarino LJ. 2008. Characterization of the human skeletal muscle proteome by one-dimensional gel electrophoresis and HPLC-ESI-MS/MS. Mol Cell Proteom 7:257–67.
73. Honikel KO. 2014. Conversion of muscle to meat—glycolysis. In: Dikeman M, Devine C, editors. Encyclopedia of meat sciences. 2nd ed. Oxford: Academic Press. p 353–7.
74. Huang F, Huang M, Xu X, Zhou G. 2011. Influence of heat on protein degradation, ultrastructure and eating quality indicators of pork. J Sci Food Agric 91:443–8.
75. Huang H, Larsen MR, Palmisano G, Dai J, Lametsch R. 2014. Quantitative phosphoproteomic analysis of porcine muscle within 24 h postmortem. J Proteom 106:125–39.
76. Huff-Lonergan E, Lonergan SM. 2005. Mechanisms of water-holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Sci 71:194–204.
77. Huff-Lonergan E, Mitsuhashi T, Beekman DD, Parrish FC, Olson DG, Robson RM. 1996. Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J Anim Sci 74:993–1008.
78. Huff-Lonergan E, Zhang W, Lonergan SM. 2010. Biochemistry of post-mortem muscle—lessons on mechanisms of meat tenderization. Meat Sci 86:184–95.
79. Hughes JM, Oiseth SK, Purslow PP, Warner RD. 2014. A structural approach to understanding the interactions between colour, water-holding capacity and tenderness. Meat Sci 98:520–32.
80. Hunt MC, Sørheim O, Slinde E. 1999. Color and heat denaturation of myoglobin forms in ground beef. J Food Sci 64:847–51.
81. Jung E-Y, Hwang Y-H, Joo S-T. 2016. The relationship between chemical compositions, meat quality, and palatability of the 10 primal cuts from Hanwoo steer. Korean J Food Sci Anim Resour 36:145–51.
82. Kajak-Siemaszko K, Aubry L, Peyrin F, Bax ML, Gatellier P, Astruc T, Przybylski W, Jaworska D, Gaillard-Martinie B, Santé-Lhoutellier V. 2011. Characterization of protein aggregates following a heating and freezing process. Food Res Intl 44:3160–6.
83. Kakade ML, Evans RJ. 1966. Chemical and enzymatic determinations of available lysine in raw and heated navy beans (Phaseolus vulgaris). Can J Biochem 44:648–50.
84. Kataoka H, Miyake M, Nishioka S, Matsumoto T, Saito K, Mitani K. 2010. Formation of protein adducts of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine in cooked foods. Mol Nutr Food Res 54:1039–48.
85. Kaur L, Maudens E, Haisman DR, Boland MJ, Singh H. 2014. Microstructure and protein digestibility of beef: the effect of cooking conditions as used in stews and curries. LWT - Food Sci Technol 55:612–20.
86. Kemp CM, Sensky PL, Bardsley RG, Buttery PJ, Parr T. 2010. Tenderness—an enzymatic view. Meat Sci 84:248–56.
87. Kemp RM, North MF, Leath SR. 2009. Component heat capacities for lamb, beef and pork at elevated temperatures. J Food Engr 92:280–4.
88. King NLR. 1978. Isoelectric variants of actin in raw and cooked meat. Meat Sci 2:313–21.
89. Kolczak T, Krzysztoforski K, Palka K. 2008. Effect of post-mortem ageing, method of heating and reheating on collagen solubility, shear force and texture parameters of bovine muscles. Pol J Food Nutr Sci 58:27–32.
90. Kong F, Tang J, Lin M, Rasco B. 2008. Thermal effects on chicken and salmon muscles: tenderness, cook loss, area shrinkage, collagen solubility and microstructure. LWT - Food Sci Technol 41:1210–22.
91. Lametsch R, Larsen MR, Essén-Gustavsson B, Jensen-Waern M, Lundström K, Lindahl G. 2011. Post-mortem changes in pork muscle protein phosphorylation in relation to the RN genotype. J Agric Food Chem 59:11608–15.
92. Lana A, Zolla L. 2016. Proteolysis in meat tenderization from the point of view of each single protein: a proteomic perspective. J Proteom 147:85–97.
93. Lawrie RA, Ledward DA. 2006a. Chapter 4—chemical and biochemical constitution of muscle. In: Lawrie RA, Ledward DA, editors. Lawrie's meat science. 7th ed. England, Cambridge: Woodhead Publishing. p 75–127.
94. Lawrie RA, Ledward DA. 2006b. Chapter 8—the storage and preservation of meat: II Moisture control. In: Lawrie RA, Ledward DA, editors. Lawrie's meat science. 7th ed. England, Cambridge: Woodhead Publishing. p 235–63.
95. Lawrie RA, Ledward DA. 2006c. Chapter 10—the eating quality of meat. In: Lawrie RA, Ledward DA, editors. Lawrie's meat science. 7th ed. England, Cambridge: Woodhead Publishing. p 279–341.
96. Lawrie RA, Ledward DA. 2006d. Chapter 11—meat and human nutrition. In: Lawrie RA, Ledward DA, editors. Lawrie's meat science. 7th ed. England, Cambridge: Woodhead Publishing. p 342–57.
97. Li ZL, Mo L, Le G, Shi Y. 2014. Oxidized casein impairs antioxidant defense system and induces hepatic and renal injury in mice. Food Chem Toxicol 64:86–93.
98. Linke WA, Krüger M. 2010. The giant protein titin as an integrator of myocyte signaling pathways. Physiology 25:186–98.
99. Liu Z, Xiong YL, Chen J. 2010. Protein oxidation enhances hydration but suppresses water-holding capacity in porcine longissimus muscle. J Agric Food Chem 58:10697–704.
100. Matsuishi M, Okitani A. 2000. Elucidation of a basic protein, glyceraldehyde-3-phosphate dehydrogenase, as a contributing factor to raise Mg-ATPase activity of myofibrils during meat conditioning. Meat Sci 56:369–77.
101. McCormick RJ. 1994. The flexibility of the collagen compartment of muscle. Meat Sci 36:79–91.
102. Meltretter J, Wüst J, Pischetsrieder M. 2013. Comprehensive analysis of nonenzymatic post-translational β-lactoglobulin modifications in processed milk by ultrahigh-performance liquid chromatography–tandem mass spectrometry. J Agric Food Chem 61:6971–81.
103. Meltretter J, Wüst J, Pischetsrieder M. 2014. Modified peptides as indicators for thermal and nonthermal reactions in processed milk. J Agric Food Chem 62:10903–15.
104. Milkovska-Stamenova S, Hoffmann R. 2016. Hexose-derived glycation sites in processed bovine milk. J Proteomics 134:102–11.
105. Milligan RA. 1996. Protein-protein interactions in the rigor actomyosin complex. Proc Natl Acad Sci USA 93:21–6.
106. Montowska M, Pospiech E. 2013. Species-specific expression of various proteins in meat tissue: proteomic analysis of raw and cooked meat and meat products made from beef, pork and selected poultry species. Food Chem 136:1461–9.
107. Mori B, Nakatsuji H. 1977. Utilization in rats of 14C-L-lysine-labeled casein browned by amino-carbonyl reaction. Agric Biol Chem 41:345–50.
108. Mudalal S, Babini E, Cavani C, Petracci M. 2014. Quantity and functionality of protein fractions in chicken breast fillets affected by white striping. Poul Sci 93:2108–16.
109. Mueller GA, Maleki SJ, Johnson K, Hurlburt BK, Cheng H, Ruan S, Nesbit JB, Pomés A, Edwards LL, Schorzman A, Deterding LJ, Park H, Tomer KB, London RE, Williams JG. 2013. Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products. Allergy 68:1546–54.
110. Nazar DS, Persson G, Olin T, Waters S, von der Decken A. 1991. Sarcoplasmic and myofibrillar proteins in white trunk muscle of salmon (Salmo salar) after estradiol treatment. Comp Biochem Physiol Part B: Comp Biochem 98:109–14.
111. Oberli M, Marsset-Baglieri A, Airinei G, Santé-Lhoutellier V, Khodorova N, Rémond D, Foucault-Simonin A, Piedcoq J, Tomé D, Fromentin G, Benamouzig R, Gaudichon C. 2015. High true ileal digestibility but not postprandial utilization of nitrogen from bovine meat protein in humans is moderately decreased by high-temperature, long-duration cooking. J Nutr 45:2221–8.
112. Oberli M, Lan A, Khodorova N, Santé-Lhoutellier V, Walker F, Piedcoq J, Davila A-M, Blachier F, Tomé D, Fromentin G, Gaudichon C. 2016. Compared with raw bovine meat, boiling but not grilling, barbecuing, or roasting decreases protein digestibility without any major consequences for intestinal mucosa in rats, although the daily ingestion of bovine meat induces histologic modifications in the colon. J Nutr 146:1506–13.
113. Ofstad R, Kidman S, Myklebust R, Hermansson A-M. 1993. Liquid holding capacity and structural changes during heating of fish muscle: cod (Gadus morhua L.) and salmon (Salmo salar). Food Struct 12:163–74.
114. Oh NS, Lee HA, Lee JY, Joung JY, Lee KB, Kim Y, Lee KW, Kim SH. 2013. The dual effects of Maillard reaction and enzymatic hydrolysis on the antioxidant activity of milk proteins. J Dairy Sci 96:4899–911.
115. Ottenheijm CAC, Granzier H. 2010. Lifting the nebula: novel insights into skeletal muscle contractility. Physiology 25:304–10.
116. Ouali A, Gagaoua M, Boudida Y, Becila S, Boudjellal A, Herrera-Mendez CH, Sentandreu MA. 2013. Biomarkers of meat tenderness: present knowledge and perspectives in regards to our current understanding of the mechanisms involved. Meat Sci 95:854–70.
117. Parker KC, Walsh RJ, Salajegheh M, Amato AA, Krastins B, Sarracino DA, Greenberg SA. 2009. Characterization of human skeletal muscle biopsy samples using shotgun proteomics. J Proteome Res 8:3265–77.
118. Pearson AM, Gillett TA. 1996a. Composition and nutritive value of raw materials and processed meats. In: Pearson AM, editor. Processed meats. 3rd ed. Gaithersburg, MD: Aspen. p 23–52.
119. Pearson AM, Gillett TA. 1996b. Meat cookery and cooked meat products. In: Pearson AM, editor. Processed meats. 3rd ed. Gaithersburg, MD: Aspen. p 105–25.
120. Peiretti PG, Medana C, Visentin S, Dal Bello F, Meineri G. 2012. Effect of cooking method on carnosine and its homologues, pentosidine and thiobarbituric acid-reactive substance contents in beef and turkey meat. Food Chem 132:80–5.
121. Ponce E, Linforth R, Hall M, Guerrero I, Taylor AJ. 1994. Stability of haem pigments in model systems and cooked meat. Meat Sci 38:141–51.
122. Pospiech E, Greaser ML, Mikolajczak B, Chiang W, Krzywdzińska M. 2002. Thermal properties of titin from porcine and bovine muscles. Meat Sci 62:187–92.
123. Poulsen MW, Hedegaard RV, Andersen JM, de Courten B, Bügel S, Nielsen J, Skibsted LH, Dragsted LO. 2013. Advanced glycation endproducts in food and their effects on health. Food Chem Toxicol 60:10–37.
124. Promeyrat A, Bax ML, Traoré S, Aubry L, Santé-Lhoutellier V, Gatellier P. 2010a. Changed dynamics in myofibrillar protein aggregation as a consequence of heating time and temperature. Meat Sci 85:625–31.
125. Promeyrat A, Gatellier P, Lebret B, Kajak-Siemaszko K, Aubry L, Santé-Lhoutellier V. 2010b. Evaluation of protein aggregation in cooked meat. Food Chem 121:412–7.
126. Promeyrat A, Sayd T, Laville E, Chambon C, Lebret B, Gatellier P. 2011. Early post-mortem sarcoplasmic proteome of porcine muscle related to protein oxidation. Food Chem 127:1097–104.
127. Promeyrat A, Daudin JD, Astruc T, Danon J, Gatellier P. 2013a. Kinetics of protein physicochemical changes induced by heating in meat using mimetic models: (2) effects of fibre type, peroxides and antioxidants. Food Chem 138:2283–90.
128. Promeyrat A, Daudin JD, Gatellier P. 2013b. Kinetics of protein physicochemical changes induced by heating in meat using mimetic models: (1) relative effects of heat and oxidants. Food Chem 138:581–9.
129. Purslow PP. 1999. The intramuscular connective tissue matrix and cell-matrix interactions in relation to meat toughness. Proceedings of the 45th International Congress of Meat Science and Technology; 1999 August 1–6; Yokohama, Japan: Japan Society for Meat Science and Technology.
130. Renzone G, Arena S, Scaloni A. 2015. Proteomic characterization of intermediate and advanced glycation end-products in commercial milk samples. J Proteomics 117:12–23.
131. Rodriguez-Estrada MT, Penazzi G, Caboni MF, Bertacco G, Lercker G. 1997. Effect of different cooking methods on some lipid and protein components of hamburgers. Meat Sci 45:365–75.
132. Roldan M, Antequera T, Armenteros M, Ruiz J. 2014. Effect of different temperature-time combinations on lipid and protein oxidation of sous-vide cooked lamb loins. Food Chem 149:129–36.
133. Rombouts I, Lagrain B, Brunnbauer M, Koehler P, Brijs K, Delcour JA. 2011. Identification of isopeptide bonds in heat-treated wheat gluten peptides. J Agric Food Chem 59:1236–43.
134. Rombouts I, Lambrecht MA, Carpentier SC, Delcour JA. 2016. Identification of lanthionine and lysinoalanine in heat-treated wheat gliadin and bovine serum albumin using tandem mass spectrometry with higher-energy collisional dissociation. Amino Acid 48:959–971.
135. Sanes JR. 2003. The basement membrane/basal lamina of skeletal muscle. J Biol Chem 278:12601–4.
136. Santé-Lhoutellier V, Astruc T, Marinova P, Greve E, Gatellier P. 2008. Effect of meat cooking on physicochemical state and in vitro digestibility of myofibrillar proteins. J Agric Food Chem 56:1488–94.
137. Sarah SA, Karsani SA, Amin I, Mokhtar NFK, Sazili AQ. 2013. Differences in thermostable actin profile of goat meat as observed in two-dimensional gel electrophoresis (2DE). Intl Food Res J 20:897–901.
138. Sarah SA, Karsani SA, Amin I, Mokhtar NFK, Sazili AQ. 2014. A proteomic based assessment on changes in myofibrillar proteins of goat longissimus muscle as affected by heat treatments. J Anim Plant Sci 24:406–12.
139. Sayd T, Chambon C, Santé-Lhoutellier V. 2016. Quantification of peptides released during in vitro digestion of cooked meat. Food Chem 197(Part B):1311–23.
140. Schiaffino S, Reggiani C. 1996. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiologic Rev 76:371–423.
141. Schmidt GR. 1988. Processing. In: Cross HR, Overby AJ, editors. World animal science. Vol. B3, Meat science, milk science and technology. London: Elsevier Science Publishers. p 83–114.
142. Sentandreu MA, Fraser PD, Halket J, Patel R, Bramley PM. 2010. A proteomic-based approach for detection of chicken in meat mixes. J Proteome Res 9:3374–83.
143. Sikes A, Tornberg E, Tume R. 2010. A proposed mechanism of tenderising post-rigor beef using high pressure–heat treatment. Meat Sci 84:390–9.
144. Simat TJ, Steinhart H. 1998. Oxidation of free tryptophan and tryptophan residues in peptides and proteins. J Agric Food Chem 46:490–8.
145. Simonetti A, Gambacorta E, Perna A. 2016. Antioxidative and antihypertensive activities of pig meat before and after cooking and in vitro gastrointestinal digestion: comparison between Italian autochthonous pig Suino Nero Lucano and a modern crossbred pig. Food Chem 212:590–5.
146. Soglia F, Petracci M, Ertbjerg P. 2016. Novel DNPH-based method for determination of protein carbonylation in muscle and meat. Food Chem 197(Part A):670–5.
147. Soladoye OP, Juárez ML, Aalhus JL, Shand P, Estévez M. 2015. Protein oxidation in processed meat: mechanisms and potential implications on human health. Comp Rev Food Sci Food Safety 14:106–22.
148. Spakovszky ZS, Greitzer EM. 2002. 16.050 Thermal energy, Fall 2002—Fundamentals of Heat Transfer. Massachusetts Institute of Technology: MIT OpenCouseWare. Available from: http://ocw.mit.edu/courses/aeronautics-and-astronautics/16-050-thermal-energy-fall-2002/lecture-notes/. License: Creative Commons BY-NC-SA. Accessed 2014 November 30.
149. Suman SP, Joseph P. 2013. Myoglobin chemistry and meat color. Annu Rev Food Sci Technol 4:79–99.
150. Sun X, Tang J, Wang J, Rasco BA, Lai K, Huang Y. 2015. Formation of advanced glycation endproducts in ground beef under pasteurisation conditions. Food Chem 172:802–7.
151. Sun X, Tang J, Wang J, Rasco BA, Lai K, Huang Y. 2016. Formation of free and protein-bound carboxymethyllysine and carboxyethyllysine in meats during commercial sterilization. Meat Sci 116:1–7.
152. Sun XD, Holley RA. 2011. Factors influencing gel formation by myofibrillar proteins in muscle foods. Comp Rev Food Sci Food Safety 10:33–51.
153. Świeca M, Sęczyk Ł, Gawlik-Dziki U, Dziki D. 2014. Bread enriched with quinoa leaves—the influence of protein–phenolics interactions on the nutritional and antioxidant quality. Food Chem 162:54–62.
154. Talamo F, D'Ambrosio C, Arena S, Del Vecchio P, Ledda L, Zehender G, Ferrara L, Scaloni A. 2003. Proteins from bovine tissues and biological fluids: defining a reference electrophoresis map for liver, kidney, muscle, plasma and red blood cells. Proteomics 3:440–60.
155. Tian X, Wu W, Yu Q, Hou M, Jia F, Li X, Dai R. 2016. Quality and proteome changes of beef m.longissimus dorsi cooked using a water bath and ohmic heating process. Innov Food Sci Emerg Technol 34:259–66.
156. Tornberg E. 2005. Effects of heat on meat proteins—implications on structure and quality of meat products. Meat Sci 70:493–508.
157. Tornberg E. 2013. Engineering processes in meat products and how they influence their biophysical properties. Meat Sci 95:871–8.
158. Traore S, Aubry L, Gatellier P, Przybylski W, Jaworska D, Kajak-Siemaszko K, Santé-Lhoutellier V. 2012a. Effect of heat treatment on protein oxidation in pig meat. Meat Sci 91:14–21.
159. Traore S, Aubry L, Gatellier P, Przybylski W, Jaworska D, Kajak-Siemaszko K, Santé-Lhoutellier V. 2012b. Higher drip loss is associated with protein oxidation. Meat Sci 90:917–24.
160. Trevisan AJB, de Almeida Lima D, Sampaio GR, Soares RAM, Markowicz Bastos DH. 2016. Influence of home cooking conditions on Maillard reaction products in beef. Food Chem 196:161–9.
161. Turesky RJ, Skipper PL, Tannenbaum SR. 1987. Binding of 2-amino-3-methylimidazo[4,5-f]quinoline to hemoglobin and albumin in vivo in the rat. Identification of an adduct suitable for dosimetry. Carcinogenesis 8:1537–42.
162. van Boekel MAJS. 1998. Effect of heating on Maillard reactions in milk. Food Chem 62:403–14.
163. Villaverde A, Estévez M. 2013. Carbonylation of myofibrillar proteins through the Maillard pathway: effect of reducing sugars and reaction temperature. J Agric Food Chem 61:3140–7.
164. Voutila L, Mullen AM, Ruusunen M, Troy D, Puolanne E. 2007. Thermal stability of connective tissue from porcine muscles. Meat Sci 76:474–80.
165. Vujadinović D, Grujić R, Tomović V, Torbica A. 2014. Effects of temperature and method of heat treatment on myofibrillar proteins of pork. Chem Ind Chem Engr Q 20: 407–15.
166. Wada Y, Lönnerdal B. 2014a. Bioactive peptides derived from human milk proteins—mechanisms of action. J Nutr Biochem 25:503–14.
167. Wada Y, Lönnerdal B. 2014b. Effects of different industrial heating processes of milk on site-specific protein modifications and their relationship to in vitro and in vivo digestibility. J Agric Food Chem 62:4175–85.
168. Wada Y, Lönnerdal B. 2015. Effects of industrial heating processes of milk-based enteral formulas on site-specific protein modifications and their relationship to in vitro and in vivo protein digestibility. J Agric Food Chem 63:6787–98.
169. Wang W-Q, Bao Y-H, Chen Y. 2013. Characteristics and antioxidant activity of water-soluble Maillard reaction products from interactions in a whey protein isolate and sugars system. Food Chem 139:355–61.
170. Warriss PD. 2010. Post-mortem changes in muscle and its conversion into meat. In: Warriss PD, editor. Meat science: an introductory text. 2nd ed. Wallingford, UK; Cambridge, Mass.: CABI. p 65–76.
171. Wen S, Zhou G, Li L, Xu X, Yu X, Bai Y, Li C. 2015. Effect of cooking on in vitro digestion of pork proteins: a peptidomic perspective. J Agric Food Chem 63: 250–261.
172. Wilkinson BHP, Lee E, Purchas RW, Morel PCH. 2014. The retention and recovery of amino acids from pork longissimus muscle following cooking to either 60 °C or 75 °C. Meat Sci 96:361–5.
173. Wood JD, Jones RCD, Francombe MA, Whelehan OP. 1986. The effects of fat thickness and sex on pig meat quality with special reference to the problems associated with overleanness 2. Laboratory and trained taste panel results. Anim Sci 43:535–44.
174. Wright DJ, Wilding P. 1984. Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments. J Sci Food Agric 35:357–72.
175. Wright DJ, Leach IB, Wilding P. 1977. Differential scanning calorimetric studies of muscle and its constituent proteins. J Sci Food Agric 28:557–64.
176. Wu G, Clerens S, Farouk MM. 2014a. LC MS/MS identification of large structural proteins from bull muscle and their degradation products during post mortem storage. Food Chem 150:137–44.
177. Wu G, Farouk MM, Clerens S, Rosenvold K. 2014b. Effect of beef ultimate pH and large structural protein changes with aging on meat tenderness. Meat Sci 98:637–45.
178. Wust J, Pischetsrieder M. 2016. Methionine sulfoxide profiling of milk proteins to assess the influence of lipids on protein oxidation in milk. Food Funct 7:2526–36.
179. Wyness L, Weichselbaum E, O'Connor A, Williams EB, Benelam B, Riley H, Stanner S. 2011. Red meat in the diet: an update. Nutr Bull 36:34–77.
180. Xiong YL. 2000. Meat processing. In: Nakai S, Modler HW, editors. Food proteins: processing applications. New York, N.Y.; Chichester: Wiley-VCH. p 89–146.
181. Xiong YL. 2014. Chemical and physical characteristics of meat—protein functionality. In: Dikeman M, Devine C, editors. Encyclopedia of meat sciences. 2nd ed. Oxford: Academic Press. p 267–73.
182. Yu T-Y, Morton JD, Clerens S, Dyer JM. 2015a. In-depth characterisation of the lamb meat proteome from longissimus lumborum. EuPA Open Proteomics 6:28–41.
183. Yu T-Y, Morton JD, Clerens S, Dyer JM. 2015b. Proteomic investigation of protein profile changes and amino acid residue level modification in cooked lamb meat: the effect of boiling. J Agric Food Chem 63:9112–23.
184. Yu T-Y, Morton JD, Clerens S, Dyer JM. 2016. Proteomic investigation of protein profile changes and amino acid residue-level modification in cooked lamb longissimus thoracis et lumborum: the effect of roasting. Meat Sci 119:80–8.
185. Zhang Q, Ames JM, Smith RD, Baynes JW, Metz TO. 2008. A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic disease. J Proteome Res 8:754–69.
186. Zhang SX, Farouk MM, Young OA, Wieliczko KJ, Podmore C. 2005. Functional stability of frozen normal and high pH beef. Meat Sci 69:765–72.
187. Zhang Y, Fonslow BR, Shan B, Baek M-C, Yates JR. 2013. Protein analysis by shotgun/bottom-up proteomics. Chem Rev 113:2343–94.