Phosphorylation of sarcoplasmic and myofibrillar proteins in three ovine muscles during postmortem ageing

doi:10.1016/S2095-3119(19)62653-5

Journal of Integrative Agriculture ›› 2019, Vol. 18 ›› Issue (7): 1643-1651.DOI: 10.1016/S2095-3119(19)62653-5

收稿日期:2018-09-05 修回日期:2019-01-29 出版日期:2019-07-01 发布日期:2019-07-01

Phosphorylation of sarcoplasmic and myofibrillar proteins in three ovine muscles during postmortem ageing

WANG Ying^{1, 2}, LI Xin², LI Zheng², DU Man-ting², ZHU Jie¹, ZHANG She-qi¹, ZHANG De-quan²

¹ Laboratory of Biomechanics and Engineering, Institute of Biophysics and College of Science, Northwest A&F University, Yangling 712100, P.R.China
² Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, P.R.China

Received:2018-09-05 Revised:2019-01-29 Online:2019-07-01 Published:2019-07-01
Contact: Correspondence ZHANG De-quan, E-mail: dequan_zhang0118@126.com; ZHU Jie, E-mail: jiezhu@nwafu.edu.cn; ZHANG She-qi, Tel: +86-29-8709240, E-mail: zhangsheqi@nwafu.edu.cn
About author:WANG Ying, E-mail: wywendy8899@126.com;
Supported by:
This study was funded by the National Agricultural Science and Technology Innovation Program in China.

摘要/Abstract

Abstract:

This study aimed to examine changes in phosphorylation of sarcoplasmic and myofibrillar proteins from longissimus lumborum, semitendinosus, and psoas major muscles during postmortem ageing for 5 d. These sarcoplasmic and myofibrillar proteins were separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with phosphorous and protein specific stains. Myofibril fragmentation index, pH, the content of lactic acid and the relative activity of μ-calpain in three ovine muscles were measured. These results showed that the relative phosphorylation level of sarcoplasmic and myofibrillar proteins of psoas major muscle were lower compared with longissimus lumborum and semitendinosus muscles (P<0.05). The pH of psoas major muscle was the lowest at 0.5 h postmortem, and the highest after 12 h postmortem (P<0.05). In addition, the relative activity of μ-calpain was higher within 5 d postmortem and myofibril fragmentation index was higher after 1 d postmortem in psoas major muscle than those of longissimus lumborum and semitendinosus muscles (P<0.05). The sarcoplasmic protein phosphorylation may regulate the rate of pH decline to influence the μ-calpain activity and then proteolysis of proteins consequently. This study gives a new perspective of the mechanism of postmortem meat tenderization.

Key words: ovine muscle , protein phosphorylation , μ-calpain , myofibril fragmentation index

. [J]. Journal of Integrative Agriculture, 2019, 18(7): 1643-1651.

WANG Ying, LI Xin, LI Zheng, DU Man-ting, ZHU Jie, ZHANG She-qi, ZHANG De-quan. Phosphorylation of sarcoplasmic and myofibrillar proteins in three ovine muscles during postmortem ageing[J]. Journal of Integrative Agriculture, 2019, 18(7): 1643-1651.

参考文献

Aliani M, Farmer L J, Kennedy J T, Moss B W, Gordon A. 2013. Post-slaughter changes in ATP metabolites, reducing and phosphorylated sugars in chicken meat. Meat Science, 94, 55–62.
Brandstetter A M, Sauerwein H, Veerkam J H, Geay Y, Hocquette J F. 2002. Effects of muscle type, castration, age and growth rate on HFABP expression in bovine skeletal muscle. Livestock Production Science, 75, 199–208.
Chen L J, Li X, Ni N, Liu Y, Chen L, Wang Z Y, Zhang D Q. 2016. Phosphorylation of myofibrillar proteins in post-mortem ovine muscle with different tenderness. Journal of Science Food Agriculture, 96, 1474–1483.
Culler R D, Smith G C, Cross H R. 1978. Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus muscle. Journal of Food Science, 43, 1177–1180.
Du M T, Li X, Li Z, Li M, Gao L L, Zhang D Q. 2017. Phosphorylation inhibits the activity of μ-calpain at different incubation temperatures and Ca2+ concentrations in vitro. Food Chemistry, 228, 649–655.
Goll D E, Thompson V F, Li H, Wei W, Cong J. 2003. The calpain system. Physiological Reviews, 83, 731–801.
Hopkins D L, Thompson J M. 2002. The degradation of myofibrillar proteins in beef and lamb using denaturing electrophoresis - An overview. Journal of Muscle Foods, 13, 81–102.
Huang H G, Larsen M R, Karlsson A H, Pomponio L, Costa L N, Lametsch R. 2011. Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics, 11, 4063–4076.
Huff-Lonergan E, Zhang W, Lonergan S M. 2010. Biochemistry of postmortem muscle - Lessons on mechanisms of meat tenderization. Meat Science, 86, 184–195.
Lametsch R, Roepstorff P, Moller H S, Bendixen E. 2004. Identification of myofibrillar substrates for μ-calpain. Meat Science, 68, 515–521.
Li C B, Zhou G H, Xu X L, Lundström K, Karlsson A, Lametesch R. 2015. Phosphoproteome analysis of sarcoplasmic and myofibrillar proteins in bovine longissimus muscle in response to postmortem electrical stimulation. Food Chemistry, 175, 197–202.
Li M, Li X, Xin J Z, Li Z, Li G X, Zhang Y, Du M T, Shen Q W, Zhang D Q. 2017. Effects of protein phosphorylation on color stability of ground meat. Food Chemistry, 219, 304–310.
Li M, Li Z, Li X, Xin J Z, Wang Y, Li G X, Wu L G, Shen Q W, Zhang D Q. 2018. Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability. Food Chemistry, 240,104–111.
Li Z, Li X, Gao X, Shen Q W, Du M T, Zhang D Q. 2017. Phosphorylation prevents in vitro myofibrillar proteins degradation by μ-calpain. Food Chemistry, 218, 455–462.
Lomiwes D, Farouk M M, Wu G, Young O A. 2014. The development of meat tenderness is likely to be compartmentalized by ultimate pH. Meat Science, 96, 646–651.
Macek B, Mann M, Olsen J V. 2009. Global and site-specific quantitative phosphoproteomics: principles and applications. Annual Review of Pharmacology & Toxicology, 49, 199–223.
Marino R, Albenzio M, Malva A, Santillo A, Loizzo P, Sevi A. 2013. Proteolytic pattern of myofibrillar protein and meat tenderness as affected by breed and aging time. Meat Science, 95, 281–287.
Marino R, Della M A, Albenzio M. 2015. Proteolytic changes of myofibrillar proteins in Podolian meat during aging: focusing on tenderness. Journal of Animal Science, 93, 1376–1387.
Mattio D V N，Paredi M E, Crupkin M. 1992. Post mortem changes in glycogen, ATP, hypoxanthine and 260/250 absorbance ratio in extracts of adductor muscles from Aulacomya ater ater (Molina) at different biological conditions. Comparative Biochemistry & Physiology (Part A: Physiology), 103, 605–608.
Melody J J, Lonergan S M, Rowe L J, Huiatt T W, Mayes M S, Huff-Lonergan E. 2004. Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. Journal of Animal Science, 82, 1195–1205.
Moczkowska M, Poltorak A, Wierzbicka A. 2017. The effect of ageing on changes in myo?brillar protein in selected muscles in relation to the tenderness of meat obtained from cross-breed heifers. International Journal of Food Science and Technology, 52, 1375–1382.
Moeller S J, Miller R K, Edwards K K, Zerby H N, Logan K E, Aldredge T L, Stahl C A, Boggess M, Box-Steffensmeier J M. 2010. Consumer perceptions of pork eating quality as affected by pork quality attributes and end-point cooked temperature. Meat Science, 84, 14–22.
Scheffler T L, Gerrard D E. 2007. Mechanisms controlling pork quality development: The biochemistry controlling postmortem energy metabolism. Meat Science, 77, 7–16.
Shen Q W, Means W J, Thompson S A, Underwood K R, Zhu M J, McCormick R J, Ford S P, Du M. 2006. Pre-slaughter transport, AMP-activated protein kinase, glycolysis, and quality of pork loin. Meat Science, 74, 388–395.
Smulder F J M, Marsh B B, Swartz R L, Russell R L, Honenecke M E. 1990. Beef tenderness and sarcomere length. Meat Science, 28, 349–363.
Veiseth-Kent E, Pedersen M E, Rønning S B, Rødbotten R. 2017. Can postmortem proteolysis explain tenderness differences in various bovine muscles? Meat Science, 137, 114–122.
Wang Y, Li X, Li Z, Li M, Zhu J, Zhang D Q. 2018. Changes in phosphorylation levels and degradation of titin in three ovine muscles during post-mortem ageing. International Journal of Food Science Technology, 53, 913–920.

Phosphorylation of sarcoplasmic and myofibrillar proteins in three ovine muscles during postmortem ageing

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