Abstract
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 pH45 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.
| Original language | English |
|---|---|
| Pages (from-to) | 183-191 |
| Number of pages | 9 |
| Journal | Livestock Science |
| Volume | 127 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 2010 Feb 1 |
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Keywords
- Muscle fiber types
- Myosin isoforms
- Pork quality
- Postmortem protein changes
- Protein denaturation
ASJC Scopus subject areas
- Animal Science and Zoology
- veterinary(all)
Cite this
Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle. / Choi, Y. M.; Lee, S. H.; Choe, J. H.; Rhee, Min-Suk; Lee, S. K.; Joo, S. T.; Kim, Byoung-Chul.
In: Livestock Science, Vol. 127, No. 2-3, 01.02.2010, p. 183-191.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Protein solubility is related to myosin isoforms, muscle fiber types, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle
AU - Choi, Y. M.
AU - Lee, S. H.
AU - Choe, J. H.
AU - Rhee, Min-Suk
AU - Lee, S. K.
AU - Joo, S. T.
AU - Kim, Byoung-Chul
PY - 2010/2/1
Y1 - 2010/2/1
N2 - 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 pH45 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.
AB - 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 pH45 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.
KW - Muscle fiber types
KW - Myosin isoforms
KW - Pork quality
KW - Postmortem protein changes
KW - Protein denaturation
UR - http://www.scopus.com/inward/record.url?scp=73949142201&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=73949142201&partnerID=8YFLogxK
U2 - 10.1016/j.livsci.2009.09.009
DO - 10.1016/j.livsci.2009.09.009
M3 - Article
AN - SCOPUS:73949142201
VL - 127
SP - 183
EP - 191
JO - Livestock Science
JF - Livestock Science
SN - 1871-1413
IS - 2-3
ER -