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

C B Li, J Li, G H Zhou, R Lametsch, Per Ertbjerg, D A Brüggemann, H G Huang, A H Karlsson, M Hviid, K Lundström

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

Sammanfattning

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, β-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.
Originalspråkengelska
TidskriftJournal of Animal Science
Volym90
Utgåva5
Sidor (från-till)1638-1649
Antal sidor12
ISSN0021-8812
DOI
StatusPublicerad - 2012
MoE-publikationstypA1 Tidskriftsartikel-refererad

Vetenskapsgrenar

  • 416 Livsmedelsvetenskap

Citera det här

Li, C B ; Li, J ; Zhou, G H ; Lametsch, R ; Ertbjerg, Per ; Brüggemann, D A ; Huang, H G ; Karlsson, A H ; Hviid, M ; Lundström, K. / Electrical stimulation affects metabolic enzyme phosphorylation, protease activation and meat tenderization in beef. I: Journal of Animal Science. 2012 ; Vol. 90, Nr. 5. s. 1638-1649.
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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, β-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.",
keywords = "416 Food Science, electrical stimulation, lysosomal enzymes, phosphorylation, proteomics, tenderization, μ-calpain",
author = "Li, {C B} and J Li and Zhou, {G H} and R Lametsch and Per Ertbjerg and Br{\"u}ggemann, {D A} and Huang, {H G} and Karlsson, {A 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",
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Li, CB, Li, J, Zhou, GH, Lametsch, R, Ertbjerg, P, Brüggemann, DA, Huang, HG, 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, nr. 5, s. 1638-1649. https://doi.org/10.2527/jas.2011-4514

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

I: Journal of Animal Science, Vol. 90, Nr. 5, 2012, s. 1638-1649.

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

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, R

AU - Ertbjerg, Per

AU - Brüggemann, D A

AU - Huang, H G

AU - Karlsson, A 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, β-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, β-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.

KW - 416 Food Science

KW - electrical stimulation

KW - lysosomal enzymes

KW - phosphorylation

KW - proteomics

KW - tenderization

KW - μ-calpain

U2 - 10.2527/jas.2011-4514

DO - 10.2527/jas.2011-4514

M3 - Article

VL - 90

SP - 1638

EP - 1649

JO - Journal of Animal Science

JF - Journal of Animal Science

SN - 0021-8812

IS - 5

ER -