Animal Bioscience

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Seasons affect the phosphorylation of pork sarcoplasmic proteins related to meat quality

  • Zeng, Xianming (Key Laboratory of Meat Processing and Quality Control, MOE) ;
  • Li, Xiao (Key Laboratory of Meat Processing and Quality Control, MOE) ;
  • Li, Chunbao (Key Laboratory of Meat Processing and Quality Control, MOE)
  • Received : 2021.04.20
  • Accepted : 2021.07.21
  • Published : 2022.01.01
Download PDF
⟨ Previous Next ⟩

Abstract

Objective: Sarcoplasmic proteins include proteins that play critical roles in biological processes of living organisms. How seasons influence biological processes and meat quality of postmortem muscles through the regulation of protein phosphorylation remain to be investigated. In this study, the phosphorylation of sarcoplasmic proteins in pork longissimus muscle was investigated in four seasons. Methods: Sarcoplasmic proteins were extracted from 40 pork carcasses (10 for each season) and analyzed through ProQ Diamond staining for phosphorylation labeling and Sypro Ruby staining for total protein labeling. The pH of muscle, contents of glycogen and ATP were measured at 45 min, 3 h, and 9 h postmortem and the water (P2b, P21, and P22) was measured at 3 h and 9 h. Results: A total of 21 bands were detected. Band 8 (heat shock cognate 71 kDa protein; heat shock 70 kDa protein 1B) had higher phosphorylation level in summer than that in other seasons at 45 min postmortem. The phosphorylation levels of 3 Bands were significantly different between fast and normal pH decline groups (p<0.05). The phosphorylation levels of 4 bands showed negative associations with immobilized water (P21) and positive association with free water (P22). Conclusion: The phosphorylation levels of sarcoplasmic proteins involved in energy metabolism and heat stress response at early postmortem time differed depending on the seasons. These proteins include heat shock protein 70, pyruvate kinase, phosphoglucomutase-1, glucose-6-phosphate isomerase, and carbonic anhydrase 3. High temperatures in summer might result in the phosphorylation of those proteins, leading to pH decline and low water holding capacity.

Keywords

Acknowledgement

This work was funded by Ministry of Agriculture and Rural Affairs of the People's Republic of China (CARS-35) and Jiangsu Provincial Science and Technology Department (SZ-XZ2017029).

References

  1. Gregory NG. How climatic changes could affect meat quality. Food Res Int 2010;43:1866-73. https://doi.org/10.1016/j.foodres.2009.05.018
  2. O'Neill DJ, Lynch PB, Troy DJ, Buckley DJ, Kerry JP. Influence of the time of year on the incidence of PSE and DFD in Irish pigmeat. Meat Sci 2003;64:105-11. https://doi.org/10.1016/S0309-1740(02)00116-X
  3. Van de Perre V, Ceustermans A, Leyten J, Geers R. The prevalence of PSE characteristics in pork and cooked ham-effects of season and lairage time. Meat Sci 2010;86:391-7. https://doi.org/10.1016/j.meatsci.2010.05.023
  4. Van de Perre V, Permentier L, De Bie S, Verbeke G, Geers R. Effect of unloading, lairage, pig handling, stunning and season on pH of pork. Meat Sci 2010;86:931-7. https://doi.org/10.1016/j.meatsci.2010.07.019
  5. Yu JM, Tang S, Bao ED, Zhang M, Hao QQ, Yue ZH. The effect of transportation on the expression of heat shock proteins and meat quality of M. longissimus dorsi in pigs. Meat Sci 2009;83:474-8. https://doi.org/10.1016/j.meatsci.2009.06.028
  6. Zhang M, Wang D, Geng Z, et al. The level of heat shock protein 90 in pig Longissimus dorsi muscle and its relationship with meat pH and quality. Food Chem 2014;165:337-41. https://doi.org/10.1016/j.foodchem.2014.05.111
  7. Zhu LQ, Zhou G, Che H, et al. Effects of season, transportation distance and lairage time on the incidence of PSE pork. Meat Industry 2015;10:35-42.
  8. Scheffler TL, Gerrard DE. Mechanisms controlling pork quality development: The biochemistry controlling postmortem energy metabolism. Meat Sci 2007;77:7-16. https://doi.org/10.1016/j.meatsci.2007.04.024
  9. Sprang SR, Acharya KR, Goldsmith EJ, et al. Structural changes in glycogen phosphorylase induced by phosphorylation. Nature 1988;336:215-21. https://doi.org/10.1038/336215a0
  10. 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;11:4063-76. https://doi.org/10.1002/pmic.201100173
  11. Li X, Fang T, Zong M, et al. Phosphorproteome changes of myofibrillar proteins at early post-mortem time in relation to pork quality as affected by season. J Agric Food Chem 2015;63:10287-94. https://doi.org/10.1021/acs.jafc.5b03997
  12. Li C, Zhou G, Xu X, Lundstrom K, Karlsson A, Lametsch R. Phosphoproteome analysis of sarcoplasmic and myofibrillar proteins in bovine longissimus muscle in response to postmortem electrical stimulation. Food Chem 2015;175:197202. https://doi.org/10.1016/j.foodchem.2014.11.139
  13. Li CB, Liu DY, Zhou GH, et al. Meat quality and cooking attributes of thawed pork with different low field NMR T(21). Meat Sci 2012;92:79-83. https://doi.org/10.1016/j.meatsci.2011.11.015
  14. Li CB, Li J, Zhou GH, et al. Electrical stimulation affects metabolic enzyme phosphorylation, protease activation, and meat tenderization in beef. J Anim Sci 2012;90:163849. https://doi.org/10.2527/jas.2011-4514
  15. Melling CWJ, Thorp DB, Milne KJ, Noble EG. Myocardial Hsp70 phosphorylation and PKC-mediated cardioprotection following exercise. Cell Stress Chaperones 2009;14:141-50. https://doi.org/10.1007/s12192-008-0065-x
  16. Hernando R, Manso R. Muscle fibre stress in response to exercise - Synthesis, accumulation and isoform transitions of 70-kDa heat-shock proteins. Eur J Biochem 1997;243:4607. https://doi.org/10.1111/j.1432-1033.1997.0460a.x
  17. Sommavilla R, Faucitano L, Gonyou H, et al. Season, transport duration and trailer compartment effects on blood stress indicators in pigs: relationship to environmental, behavioral and other physiological factors, and pork quality traits. Animals (Basel) 2017;7:8. https://doi.org/10.3390/ani7020008
  18. Newman D, Young J, Carr C, Ryan M, Berg E. Effect of season, transport length, deck location, and lairage length on pork quality and blood cortisol concentrations of market hogs. Animals (Basel) 2014;4:627-42. https://doi.org/10.3390/ani4040627
  19. Srivastava D, Nandi S, Dey M. Mechanistic and structural insights into cysteine-mediated inhibition of pyruvate kinase muscle isoform 2. Biochemistry 2019;58:3669-82. https://doi.org/10.1021/acs.biochem.9b00349
  20. Anderson MJ, Lonergan SM, Huff-Lonergan E. Differences in phosphorylation of phosphoglucomutase 1 in beef steaks from the longissimus dorsi with high or low star probe values. Meat Sci 2014;96:379-84. https://doi.org/10.1016/j.meatsci.2013.07.017
  21. Hallerdei J, Scheibe RJ, Parkkila S, et al. T tubules and surface membranes provide equally effective pathways of carbonic anhydrase-facilitated lactic acid transport in skeletal muscle. PLoS ONE 2010;5:e15137. https://doi.org/10.1371/journal.pone.0015137
  22. Nadeau OW, Lane LA, Xu D, et al. Structure and location of the regulatory beta subunits in the (alpha beta gamma delta)(4) phosphorylase kinase complex. J Biol Chem 2012;287:3665161. https://doi.org/10.1074/jbc.M112.412874
  23. Rhoades RD, King DA, Jenschke BE, Behrends JM, Hively TS, Smith SB. Postmortem regulation of glycolysis by 6-phosphofructokinase in bovine M. Sternocephalicus pars mandibularis. Meat Sci 2005;70:621-6. https://doi.org/10.1016/j.meatsci.2005.01.024
  24. Leite TC, Da Silva D, Coelho RG, Zancan P, Sola-Penna M. Lactate favours the dissociation of skeletal muscle 6-phosphofructo-1-kinase tetramers down-regulating the enzyme and muscle glycolysis. Biochem J 2007;408:123-30. https://doi.org/10.1042/BJ20070687
  25. Lametsch R, Roepstorff P, Bendixen E. Identification of protein degradation during post-mortem storage of pig meat. J Agric Food Chem 2002;50:5508-12. https://doi.org/10.1021/jf025555n
  26. Purintrapiban J, Wang MC, Forsberg NE. Identification of glycogen phosphorylase and creatine kinase as calpain substrates in skeletal muscle. Int J Biochem Cell Biol 2001;33:531-40. https://doi.org/10.1016/S1357-2725(01)00012-7