Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle
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Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. / Huang, Honggang; Larsen, Martin Røssel; Lametsch, Rene.
In: Food Chemistry, Vol. 134, No. 4, 2012, p. 1999-2006.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle
AU - Huang, Honggang
AU - Larsen, Martin Røssel
AU - Lametsch, Rene
PY - 2012
Y1 - 2012
N2 - A gel-based phosphoproteomic study was performed to investigate the postmortem (PM) changes in protein phosphorylation of the myofibrillar proteins in three groups of pigs with different pH decline rates, from PM 1 h to 24 h. The global phosphorylation level in the group with a fast pH decline rate was higher than that in the slow and intermediate groups at early PM time, but became the lowest at 24 h. The protein phosphorylation level of seven individual protein bands was only significantly (p<0.05) affected by PM time, and two protein bands were subjected to a synergy effect between PM time and pH decline rate. A total of 35 non-redundant highly abundant proteins were identified from 19 protein bands; most of the identified proteins were sarcomeric function-related proteins. Myosin-binding protein C, troponin T, tropomyosin and myosin regulatory light chain 2 were identified in the highly phosphorylated protein bands with the highest scores. The results indicate that the phosphorylation pattern of myofibrillar proteins in PM muscle is mainly changed with PM time, but only to a minor extent influenced by the rate of pH decline, suggesting that the phosphorylation of myofibrillar proteins may be related to the meat rigor mortis and quality development. --------------------------------------------------------------------------------
AB - A gel-based phosphoproteomic study was performed to investigate the postmortem (PM) changes in protein phosphorylation of the myofibrillar proteins in three groups of pigs with different pH decline rates, from PM 1 h to 24 h. The global phosphorylation level in the group with a fast pH decline rate was higher than that in the slow and intermediate groups at early PM time, but became the lowest at 24 h. The protein phosphorylation level of seven individual protein bands was only significantly (p<0.05) affected by PM time, and two protein bands were subjected to a synergy effect between PM time and pH decline rate. A total of 35 non-redundant highly abundant proteins were identified from 19 protein bands; most of the identified proteins were sarcomeric function-related proteins. Myosin-binding protein C, troponin T, tropomyosin and myosin regulatory light chain 2 were identified in the highly phosphorylated protein bands with the highest scores. The results indicate that the phosphorylation pattern of myofibrillar proteins in PM muscle is mainly changed with PM time, but only to a minor extent influenced by the rate of pH decline, suggesting that the phosphorylation of myofibrillar proteins may be related to the meat rigor mortis and quality development. --------------------------------------------------------------------------------
U2 - 10.1016/j.foodchem.2012.03.132
DO - 10.1016/j.foodchem.2012.03.132
M3 - Journal article
C2 - 23442649
VL - 134
SP - 1999
EP - 2006
JO - Food Chemistry
JF - Food Chemistry
SN - 0308-8146
IS - 4
ER -
ID: 37928026