Post-translational modifications (PTMs) play an important role in life science. The most widely studied protein modifications in biological science include protein phosphorylation, acylation, glycosylation, ubiquitination, acetylation, oxidation, methylation and so on. This review outlines current achievements in the study of protein modifications in muscle food using proteomic approaches. First we describe the general knowledge of protein modifications and then the development of proteomic approaches for the characterization of such modifications. Second, we describe the effects of protein modifications on muscle foods and devote our main attention to the application of proteomic approaches for the analysis of these modifications. We conclude that proteomics analysis is powerful for the study of protein modifications and analysis of meat quality characteristics in the process of food production.
Qiang Pu,Jia Luo,Linyuan Shen,Xuewei Li,Shunhua Zhang,Li Zhu
. Application of modification-specific proteomics in the meat-quality study[J]. Hereditas(Beijing), 2015
, 37(4)
: 327
-335
.
DOI: 10.16288/j.yczz.14-417
[1] Paredi G, Raboni S, Bendixen E, de Almeida AM, Mozzarelli A. “Muscle to meat” molecular events and technological transformations: The proteomics insight. J Proteomics , 2012, 75(14): 4275-4289.
[2] Lagerstedt Å, Lundström K, Lindahl G. Influence of vacuum or high-oxygen modified atmosphere packaging on quality of beef M. longissimus dorsi steaks after different ageing times. Meat Sci , 2011, 87(2): 101-106.
[3] Lund MN, Heinonen M, Baron CP, Estévez M. Protein oxidation in muscle foods: A review. Mol Nutr Food Res , 2011, 55(1): 83-95.
[4] Promeyrat A, Sayd T, Laville E, Chambon C, Lebret B, Gatellier P. Early post-mortem sarcoplasmic proteome of porcine muscle related to protein oxidation. Food Chem , 2011, 127(3): 1097-1104.
[5] Huang H, Larsen MR, Karlsson AH, Pomponio L, Costa LN, Lametsch R. Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics , 2011, 11(20): 4063-4076.
[6] Lametsch R, Larsen MR, Essén-Gustavsson B, Jensen-Waern M, Lundström K, Lindahl G. Postmortem changes in pork muscle protein phosphorylation in relation to the RN genotype. J Agric Food Chem , 2011, 59(21): 11608-11615.
[7] Koohmaraie M. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Sci , 1996, 43(Suppl. 1): 193-201.
[8] Aebersold R, Mann M. Mass spectrometry-based proteomics. Nature , 2003, 422(6928): 198-207.
[9] Yates JR, Ruse CI, Nakorchevsky A. Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng , 2009, 11: 49-79.
[10] Bendixen E, Danielsen M, Hollung K, Gianazza E, Miller I. Farm animal proteomics—a review. J Proteomics , 2011, 74(3): 282-293.
[11] Wilkins MR, Pasquali C, Appel RD, Ou K, Golaz O, Sanchez JC, Yan JX, Gooley AA, Hughes G, Humphery-Smith I. From proteins to proteomes: large scale protein identification by two-dimensional electrophoresis and arnino acid analysis. Nat Biotechnol , 1996, 14(1): 61-65.
[12] Bendixen E. The use of proteomics in meat science. Meat Sci , 2005, 71(1): 138-149.
[13] Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS. Global analysis of protein expression in yeast. Nature , 2003, 425(6959): 737-741.
[14] Jia X, Hollung K, Therkildsen M, Hildrum KI, Bendixen E. Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis . Proteomics , 2006, 6(3): 936-944.
[15] Walsh CT, Garneau-Tsodikova S, Gatto GJ Jr. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Intl Ed , 2005, 44(45): 7342-7372.
[16] Jensen ON. Interpreting the protein language using proteomics. Nat Rev Mol Cell Biol , 2006, 7(6): 391-403.
[17] Khoury GA, Baliban RC, Floudas CA. Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database. Sci Rep , 2011, 1: Article number 90.
[18] Kerwin BA, Remmele RL. Protect from light: photodegradation and protein biologics. J Pharm Sci , 2007, 96(6): 1468-1479.
[19] Promeyrat A, Gatellier P, Lebret B, Kajak-Siemaszko K, Aubry L, Santé-Lhoutellier V. Evaluation of protein aggregation in cooked meat. Food Chem , 2010, 121(2): 412-417.
[20] Shen QW, Du M. Role of AMP‐activated protein kinase in the glycolysis of postmortem muscle. J Sci Food Agric , 2005, 85(14): 2401-2406.
[21] Witze ES, Old WM, Resing KA, Ahn NG. Mapping protein post-translational modifications with mass spectrometry. Nat Methods , 2007, 4(10): 798-806.
[22] Steinberg TH, Agnew BJ, Gee KR, Leung WY, Goodman T, Schulenberg B, Hendrickson J, Beechem JM, Haugland RP, Patton WF. Global quantitative phosphoprotein analysis using multiplexed proteomics technology. Proteomics , 2003, 3(7): 1128-1144.
[23] Jensen ON. Modification
