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Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability.
Li, Meng; Li, Zheng; Li, Xin; Xin, Jianzeng; Wang, Ying; Li, Guixia; Wu, Liguo; Shen, Qingwu W; Zhang, Dequan.
Afiliación
  • Li M; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China.
  • Li Z; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China.
  • Li X; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China.
  • Xin J; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China.
  • Wang Y; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China.
  • Li G; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China.
  • Wu L; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China.
  • Shen QW; College of Food Science and Technology, Hunan Agricultural University, Changsha, Hunan 410128, PR China. Electronic address: yaoyao3153@aliyun.com.
  • Zhang D; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, PR China. Electronic address: dequan_zhang0118@126.com.
Food Chem ; 240: 104-111, 2018 Feb 01.
Article en En | MEDLINE | ID: mdl-28946221
ABSTRACT
The phosphorylation of sarcoplasmic proteins in postmortem muscles was investigated in relationship to color stability in the present study. Although no difference was observed in the global phosphorylation level of sarcoplasmic proteins, difference was determined in the phosphorylation levels of individual protein bands from muscles with different color stability. Correlation analysis and liquid chromatography - tandem mass spectrometry (LC-MS/MS) identification of phosphoproteins showed that most of the color stability-related proteins were glycolytic enzymes. Interestingly, the phosphorylation level of myoglobin was inversely related to meat color stability. As the phosphorylation of myoglobin increased, color stability based on a∗ value decreased and metMb content increased. In summary, the study revealed that protein phosphorylation might play a role in the regulation of meat color stability probably by regulating glycolysis and the redox stability of myoglobin, which might be affected by the phosphorylation of myoglobin.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Fosfoproteínas / Músculo Esquelético Límite: Animals Idioma: En Revista: Food Chem Año: 2018 Tipo del documento: Article

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Fosfoproteínas / Músculo Esquelético Límite: Animals Idioma: En Revista: Food Chem Año: 2018 Tipo del documento: Article