Influence of early pH decline on calpain activity in porcine muscle

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Influence of early pH decline on calpain activity in porcine muscle. / Pomponio, Luigi; Ertbjerg, Per; Karlsson, Anders H; Costa, Leonardo Nanni; Lametsch, Rene.

In: Meat Science, Vol. 85, No. 1, 2010, p. 110-114.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Pomponio, L, Ertbjerg, P, Karlsson, AH, Costa, LN & Lametsch, R 2010, 'Influence of early pH decline on calpain activity in porcine muscle', Meat Science, vol. 85, no. 1, pp. 110-114. https://doi.org/10.1016/j.meatsci.2009.12.013

APA

Pomponio, L., Ertbjerg, P., Karlsson, A. H., Costa, L. N., & Lametsch, R. (2010). Influence of early pH decline on calpain activity in porcine muscle. Meat Science, 85(1), 110-114. https://doi.org/10.1016/j.meatsci.2009.12.013

Vancouver

Pomponio L, Ertbjerg P, Karlsson AH, Costa LN, Lametsch R. Influence of early pH decline on calpain activity in porcine muscle. Meat Science. 2010;85(1):110-114. https://doi.org/10.1016/j.meatsci.2009.12.013

Author

Pomponio, Luigi ; Ertbjerg, Per ; Karlsson, Anders H ; Costa, Leonardo Nanni ; Lametsch, Rene. / Influence of early pH decline on calpain activity in porcine muscle. In: Meat Science. 2010 ; Vol. 85, No. 1. pp. 110-114.

Bibtex

@article{96637890251011df8ed1000ea68e967b,
title = "Influence of early pH decline on calpain activity in porcine muscle",
abstract = "This study investigated the influence of post-mortem pH decline on calpain activity and myofibrillar degradation.From 80 pigs, 30 Longissimus dorsi (LD) muscles were selected on the basis of pH values at 3 h post-mortem and classified into groups of 10 as fast, intermediate and slow pH decline. The rate of pH decline early post-mortem differed between the three groups, but the ultimate pH values were similar at 24 h. Calpain activity and autolysis from 1 to 72 h post-mortem were determined using casein zymography and studied in relation to myofibrillar fragmentation.Colour and drip loss were measured. A faster decrease in pH resulted in reduced level of l-calpain activity and increased autolysis of the enzyme, and hence an earlier loss of activity due to activation of l-calpain in muscles with a fast pH decline. Paralleling the l-calpain activation in muscles with a fast pH decline a higher myofibril fragmentation at 24 h post-mortem was observed, which was no longer evident in the later phase of the tenderization process. In conclusion, the rate of early pH decline influenced l-calpain activity and the rate but not the extent of myofibrillar degradation, suggesting an early effect of proteolysis on myofibril fragmentation that is reduced during ageing due to an earlier exhaustion of lcalpain activity.",
author = "Luigi Pomponio and Per Ertbjerg and Karlsson, {Anders H} and Costa, {Leonardo Nanni} and Rene Lametsch",
year = "2010",
doi = "10.1016/j.meatsci.2009.12.013",
language = "English",
volume = "85",
pages = "110--114",
journal = "Meat Science",
issn = "0309-1740",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Influence of early pH decline on calpain activity in porcine muscle

AU - Pomponio, Luigi

AU - Ertbjerg, Per

AU - Karlsson, Anders H

AU - Costa, Leonardo Nanni

AU - Lametsch, Rene

PY - 2010

Y1 - 2010

N2 - This study investigated the influence of post-mortem pH decline on calpain activity and myofibrillar degradation.From 80 pigs, 30 Longissimus dorsi (LD) muscles were selected on the basis of pH values at 3 h post-mortem and classified into groups of 10 as fast, intermediate and slow pH decline. The rate of pH decline early post-mortem differed between the three groups, but the ultimate pH values were similar at 24 h. Calpain activity and autolysis from 1 to 72 h post-mortem were determined using casein zymography and studied in relation to myofibrillar fragmentation.Colour and drip loss were measured. A faster decrease in pH resulted in reduced level of l-calpain activity and increased autolysis of the enzyme, and hence an earlier loss of activity due to activation of l-calpain in muscles with a fast pH decline. Paralleling the l-calpain activation in muscles with a fast pH decline a higher myofibril fragmentation at 24 h post-mortem was observed, which was no longer evident in the later phase of the tenderization process. In conclusion, the rate of early pH decline influenced l-calpain activity and the rate but not the extent of myofibrillar degradation, suggesting an early effect of proteolysis on myofibril fragmentation that is reduced during ageing due to an earlier exhaustion of lcalpain activity.

AB - This study investigated the influence of post-mortem pH decline on calpain activity and myofibrillar degradation.From 80 pigs, 30 Longissimus dorsi (LD) muscles were selected on the basis of pH values at 3 h post-mortem and classified into groups of 10 as fast, intermediate and slow pH decline. The rate of pH decline early post-mortem differed between the three groups, but the ultimate pH values were similar at 24 h. Calpain activity and autolysis from 1 to 72 h post-mortem were determined using casein zymography and studied in relation to myofibrillar fragmentation.Colour and drip loss were measured. A faster decrease in pH resulted in reduced level of l-calpain activity and increased autolysis of the enzyme, and hence an earlier loss of activity due to activation of l-calpain in muscles with a fast pH decline. Paralleling the l-calpain activation in muscles with a fast pH decline a higher myofibril fragmentation at 24 h post-mortem was observed, which was no longer evident in the later phase of the tenderization process. In conclusion, the rate of early pH decline influenced l-calpain activity and the rate but not the extent of myofibrillar degradation, suggesting an early effect of proteolysis on myofibril fragmentation that is reduced during ageing due to an earlier exhaustion of lcalpain activity.

U2 - 10.1016/j.meatsci.2009.12.013

DO - 10.1016/j.meatsci.2009.12.013

M3 - Journal article

C2 - 20374873

VL - 85

SP - 110

EP - 114

JO - Meat Science

JF - Meat Science

SN - 0309-1740

IS - 1

ER -

ID: 18314578