期刊
LIVESTOCK SCIENCE
卷 127, 期 2-3, 页码 183-191出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.livsci.2009.09.009
关键词
Protein denaturation; Myosin isoforms; Muscle fiber types; Pork quality; Postmortem protein changes
资金
- Korea University
- Agricultural R&D Promotion Center of the Republic of Korea
- Agriculture & Forestry Technology Management Center, Republic of Korea [ARPC108090-3] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [과C6A2202] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
The aim of this study was to investigate the variations in myosin heavy chain (MHC) isoform content, muscle fiber type composition. and meat quality traits in pork groups that were categorized by total protein solubility (TPS). Additionally, this study focused on individual postmortem protein changes using two-dimensional electrophoresis (2-DE) based proteome analysis in the porcine longissimus dorsi muscles categorized by TPS. The low TPS group showed higher percentages of the MHC fast isoform (P < 0.05) and fiber type IIB (P < 0.01) than the high TPS group. Moreover, muscles with a higher extent of protein denaturation showed a lower muscle pH(45 min) (P < 0.01), paler surfaces (P < 0.01), and higher degrees of fluid loss by exudation (P < 0.01), as well as greater myofibrillar and metabolic protein degradation than muscles with a lower extent of protein denaturation. This study provides new evidence that myofibrillar and metabolic protein fragmentations using 2-DE based proteome analysis, particularly that of myosin, actin, the troponin T 4f isoform, and glycogen phosphorylase fragments, are useful for explaining variations in the degree of protein denaturation, and ultimate meat quality. (C) 2009 Elsevier B.V. All rights reserved.
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