Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef

Research output: Contribution to journalJournal articlepeer-review

Standard

Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef. / Li, C.B.; Li, J.; Zhou, G.H.; Lametsch, Rene; Ertbjerg, Per; Brüggemann, Dagmar Adeline; Huang, Honggang; Karlsson, Anders H; Hviid, M.; Lundström, K.

In: Journal of Animal Science, Vol. 90, No. 5, 2012, p. 1638-1649.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Li, CB, Li, J, Zhou, GH, Lametsch, R, Ertbjerg, P, Brüggemann, DA, Huang, H, Karlsson, AH, Hviid, M & Lundström, K 2012, 'Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef', Journal of Animal Science, vol. 90, no. 5, pp. 1638-1649. https://doi.org/10.2527/jas.2011-4514

APA

Li, C. B., Li, J., Zhou, G. H., Lametsch, R., Ertbjerg, P., Brüggemann, D. A., Huang, H., Karlsson, A. H., Hviid, M., & Lundström, K. (2012). Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef. Journal of Animal Science, 90(5), 1638-1649. https://doi.org/10.2527/jas.2011-4514

Vancouver

Li CB, Li J, Zhou GH, Lametsch R, Ertbjerg P, Brüggemann DA et al. Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef. Journal of Animal Science. 2012;90(5):1638-1649. https://doi.org/10.2527/jas.2011-4514

Author

Li, C.B. ; Li, J. ; Zhou, G.H. ; Lametsch, Rene ; Ertbjerg, Per ; Brüggemann, Dagmar Adeline ; Huang, Honggang ; Karlsson, Anders H ; Hviid, M. ; Lundström, K. / Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef. In: Journal of Animal Science. 2012 ; Vol. 90, No. 5. pp. 1638-1649.

Bibtex

@article{21e94b81ed0c468886e66bbca89f7f64,
title = "Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef",
abstract = "The objective of this study was to investigate the response of sarcoplasmic proteins in bovine longissimus muscle to low-voltage electrical stimulation (ES, 80 V, 35 s) after dressing and its contribution to meat tenderization at early postmortem time. Proteome analysis showed that ES resulted in lower (P <0.05) phosphorylation levels of creatine kinase M chain, fructose bisphosphate aldolase C-A, {\ss}-enolase and pyruvate kinase at 3 h postmortem. Zymography indicated an earlier (P <0.05) activation of µ-calpain in ES muscles. Free lysosomal cathepsin B&L activity increased faster (P <0.05) in ES muscles up to 24 h. Immunohistochemistry and transmission electron microscopy further indicated that lysosomal enzymes were released at early postmortem time. ES also induced ultrastructural disruption of sarcomeres. In addition, ES accelerated (P <0.05) depletion of ATP, phosphate creatine and glycogen, as well as pH decline and more preferred pH/temperature decline mode. Finally, ES accelerated meat tenderization with lower (P <0.05) shear force values than control over testing time. A possible relationship was suggested between change in phosphorylation level of energy metabolic enzymes and postmortem tenderization of beef. Our results suggested the possible importance of activation of µ-calpain, phosphorylation of sarcoplasmic proteins and release of lysosomal enzymes for ES-induced tenderization of beef muscle.",
author = "C.B. Li and J. Li and G.H. Zhou and Rene Lametsch and Per Ertbjerg and Br{\"u}ggemann, {Dagmar Adeline} and Honggang Huang and Karlsson, {Anders H} and M. Hviid and K. Lundstr{\"o}m",
year = "2012",
doi = "10.2527/jas.2011-4514",
language = "English",
volume = "90",
pages = "1638--1649",
journal = "Journal of Animal Science",
issn = "0021-8812",
publisher = "American Society of Animal Science",
number = "5",

}

RIS

TY - JOUR

T1 - Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef

AU - Li, C.B.

AU - Li, J.

AU - Zhou, G.H.

AU - Lametsch, Rene

AU - Ertbjerg, Per

AU - Brüggemann, Dagmar Adeline

AU - Huang, Honggang

AU - Karlsson, Anders H

AU - Hviid, M.

AU - Lundström, K.

PY - 2012

Y1 - 2012

N2 - The objective of this study was to investigate the response of sarcoplasmic proteins in bovine longissimus muscle to low-voltage electrical stimulation (ES, 80 V, 35 s) after dressing and its contribution to meat tenderization at early postmortem time. Proteome analysis showed that ES resulted in lower (P <0.05) phosphorylation levels of creatine kinase M chain, fructose bisphosphate aldolase C-A, ß-enolase and pyruvate kinase at 3 h postmortem. Zymography indicated an earlier (P <0.05) activation of µ-calpain in ES muscles. Free lysosomal cathepsin B&L activity increased faster (P <0.05) in ES muscles up to 24 h. Immunohistochemistry and transmission electron microscopy further indicated that lysosomal enzymes were released at early postmortem time. ES also induced ultrastructural disruption of sarcomeres. In addition, ES accelerated (P <0.05) depletion of ATP, phosphate creatine and glycogen, as well as pH decline and more preferred pH/temperature decline mode. Finally, ES accelerated meat tenderization with lower (P <0.05) shear force values than control over testing time. A possible relationship was suggested between change in phosphorylation level of energy metabolic enzymes and postmortem tenderization of beef. Our results suggested the possible importance of activation of µ-calpain, phosphorylation of sarcoplasmic proteins and release of lysosomal enzymes for ES-induced tenderization of beef muscle.

AB - The objective of this study was to investigate the response of sarcoplasmic proteins in bovine longissimus muscle to low-voltage electrical stimulation (ES, 80 V, 35 s) after dressing and its contribution to meat tenderization at early postmortem time. Proteome analysis showed that ES resulted in lower (P <0.05) phosphorylation levels of creatine kinase M chain, fructose bisphosphate aldolase C-A, ß-enolase and pyruvate kinase at 3 h postmortem. Zymography indicated an earlier (P <0.05) activation of µ-calpain in ES muscles. Free lysosomal cathepsin B&L activity increased faster (P <0.05) in ES muscles up to 24 h. Immunohistochemistry and transmission electron microscopy further indicated that lysosomal enzymes were released at early postmortem time. ES also induced ultrastructural disruption of sarcomeres. In addition, ES accelerated (P <0.05) depletion of ATP, phosphate creatine and glycogen, as well as pH decline and more preferred pH/temperature decline mode. Finally, ES accelerated meat tenderization with lower (P <0.05) shear force values than control over testing time. A possible relationship was suggested between change in phosphorylation level of energy metabolic enzymes and postmortem tenderization of beef. Our results suggested the possible importance of activation of µ-calpain, phosphorylation of sarcoplasmic proteins and release of lysosomal enzymes for ES-induced tenderization of beef muscle.

U2 - 10.2527/jas.2011-4514

DO - 10.2527/jas.2011-4514

M3 - Journal article

C2 - 22147478

VL - 90

SP - 1638

EP - 1649

JO - Journal of Animal Science

JF - Journal of Animal Science

SN - 0021-8812

IS - 5

ER -

ID: 37927948