TY - GEN
T1 - Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference
AU - Huang, Honggang
AU - Larsen, Martin R
AU - Karlsson, Anders H
AU - Lametsch, Rene
PY - 2012
Y1 - 2012
N2 - The aim of this study was to characterize the protein phosphorylation in postmortem (PM) muscle and reveal the change during meat quality development. The gel-based phosphoproteomic analysis of PM porcine muscle was performed in three pig groups with different pH decline rates from PM 1h to 24 h. The sarcoplasmic and myofibrillar fractions were analyzed using gel electrophoresis in combination with a phosphoprotein specific staining. Globally, the group with fast pH decline rate had the highest phosphorylation level at PM 1 h, but lowest at PM 24 h, whereas the group with slow pH decline rate showed the reverse case. The phosphorylation level of 12 bands in sarcoplasmic fraction and 3 bands in myofibrillar fraction were significantly affected by the synergy effects of pH and time (p<0.05). 72 unique proteins were identified. The phosphorylation patterns of pyruvate kinase, triosephosphate isomerase-1, tropomyosin and myosin regulatory light chain 2 showed to be related to PM muscle pH decline rate and time. Our work sheds light on the potential role of protein phosphorylation on regulation of meat quality development.
AB - The aim of this study was to characterize the protein phosphorylation in postmortem (PM) muscle and reveal the change during meat quality development. The gel-based phosphoproteomic analysis of PM porcine muscle was performed in three pig groups with different pH decline rates from PM 1h to 24 h. The sarcoplasmic and myofibrillar fractions were analyzed using gel electrophoresis in combination with a phosphoprotein specific staining. Globally, the group with fast pH decline rate had the highest phosphorylation level at PM 1 h, but lowest at PM 24 h, whereas the group with slow pH decline rate showed the reverse case. The phosphorylation level of 12 bands in sarcoplasmic fraction and 3 bands in myofibrillar fraction were significantly affected by the synergy effects of pH and time (p<0.05). 72 unique proteins were identified. The phosphorylation patterns of pyruvate kinase, triosephosphate isomerase-1, tropomyosin and myosin regulatory light chain 2 showed to be related to PM muscle pH decline rate and time. Our work sheds light on the potential role of protein phosphorylation on regulation of meat quality development.
M3 - Conference article
SN - 1025-904X
JO - International Congress on Meat Science and Technology. Proceedings
JF - International Congress on Meat Science and Technology. Proceedings
ER -