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Effect of combined high pressure and thermal treatment on myofibrillar proteins solubilization of beef muscle.

Ma H, Zhou G, Ledward DA, Yu X, Pan R - Int J Mol Sci (2011)

Bottom Line: The effects of high pressure (to 600 MPa) at different temperatures (20 to 60 °C) for 20 min on protein solubilization and electrophoretic pattern in beef post-rigor longissimus dorsi muscle were studied.The results showed that protein solubilization increased with increasing temperature, especially from 40 °C to 60 °C.A regular trend of protein solubilization was found when isolated myofibrils were subjected to high pressure at different temperatures, an increase was observed with increasing pressure up to about 400 MPa, solubility then decreasing to 600 MPa.

View Article: PubMed Central - PubMed

Affiliation: School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China; E-Mails: yuxiaoling@163.com (X.Y.); prsh@hist.edu.cn (R.P.).

ABSTRACT
The effects of high pressure (to 600 MPa) at different temperatures (20 to 60 °C) for 20 min on protein solubilization and electrophoretic pattern in beef post-rigor longissimus dorsi muscle were studied. The results showed that protein solubilization increased with increasing temperature, especially from 40 °C to 60 °C. A regular trend of protein solubilization was found when isolated myofibrils were subjected to high pressure at different temperatures, an increase was observed with increasing pressure up to about 400 MPa, solubility then decreasing to 600 MPa. Electrophoretic profiles showed that myosin light chains and actin thin filaments were sensitive to pressure, and were released from myofibrils subjected to 100 MPa and higher pressures at the different temperatures.

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SDS-PAGE profiles from supernatants (A) and precipitates (B) of myofibrils after pressure treatment at 20 °C. M: myofibril; S: molecular weight standards; 1, 2, 3, 4 and 5 represent control samples and samples after treatment at 100, 200, 400, 600 MPa, respectively. MHC: myosin heavy chain; α: α-actinin; A: actin; Tn-T: troponin T; Tm: tropomyosin; Tn-I: troponin I; Tn-C: troponin C; LC1, 2, 3 represent myosin light chains 1, 2, 3, respectively.
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f2-ijms-12-03034: SDS-PAGE profiles from supernatants (A) and precipitates (B) of myofibrils after pressure treatment at 20 °C. M: myofibril; S: molecular weight standards; 1, 2, 3, 4 and 5 represent control samples and samples after treatment at 100, 200, 400, 600 MPa, respectively. MHC: myosin heavy chain; α: α-actinin; A: actin; Tn-T: troponin T; Tm: tropomyosin; Tn-I: troponin I; Tn-C: troponin C; LC1, 2, 3 represent myosin light chains 1, 2, 3, respectively.

Mentions: SDS-PAGE profiles from supernatants and precipitates of the myofibrils after pressure treatment at 20 °C are shown in Figure 2. From Figure 2 and the relative intensity of the bands (data not shown), it was found that proteins molecular weights over 41 kDa decreased in the supernatant, while proteins in the molecular weight range 35–16 kDa increased in both the supernatant and precipitate when samples were subjected to pressures over 100 MPa, due to depolymerization of the myofibrillar proteins treated at higher pressures.


Effect of combined high pressure and thermal treatment on myofibrillar proteins solubilization of beef muscle.

Ma H, Zhou G, Ledward DA, Yu X, Pan R - Int J Mol Sci (2011)

SDS-PAGE profiles from supernatants (A) and precipitates (B) of myofibrils after pressure treatment at 20 °C. M: myofibril; S: molecular weight standards; 1, 2, 3, 4 and 5 represent control samples and samples after treatment at 100, 200, 400, 600 MPa, respectively. MHC: myosin heavy chain; α: α-actinin; A: actin; Tn-T: troponin T; Tm: tropomyosin; Tn-I: troponin I; Tn-C: troponin C; LC1, 2, 3 represent myosin light chains 1, 2, 3, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3116173&req=5

f2-ijms-12-03034: SDS-PAGE profiles from supernatants (A) and precipitates (B) of myofibrils after pressure treatment at 20 °C. M: myofibril; S: molecular weight standards; 1, 2, 3, 4 and 5 represent control samples and samples after treatment at 100, 200, 400, 600 MPa, respectively. MHC: myosin heavy chain; α: α-actinin; A: actin; Tn-T: troponin T; Tm: tropomyosin; Tn-I: troponin I; Tn-C: troponin C; LC1, 2, 3 represent myosin light chains 1, 2, 3, respectively.
Mentions: SDS-PAGE profiles from supernatants and precipitates of the myofibrils after pressure treatment at 20 °C are shown in Figure 2. From Figure 2 and the relative intensity of the bands (data not shown), it was found that proteins molecular weights over 41 kDa decreased in the supernatant, while proteins in the molecular weight range 35–16 kDa increased in both the supernatant and precipitate when samples were subjected to pressures over 100 MPa, due to depolymerization of the myofibrillar proteins treated at higher pressures.

Bottom Line: The effects of high pressure (to 600 MPa) at different temperatures (20 to 60 °C) for 20 min on protein solubilization and electrophoretic pattern in beef post-rigor longissimus dorsi muscle were studied.The results showed that protein solubilization increased with increasing temperature, especially from 40 °C to 60 °C.A regular trend of protein solubilization was found when isolated myofibrils were subjected to high pressure at different temperatures, an increase was observed with increasing pressure up to about 400 MPa, solubility then decreasing to 600 MPa.

View Article: PubMed Central - PubMed

Affiliation: School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China; E-Mails: yuxiaoling@163.com (X.Y.); prsh@hist.edu.cn (R.P.).

ABSTRACT
The effects of high pressure (to 600 MPa) at different temperatures (20 to 60 °C) for 20 min on protein solubilization and electrophoretic pattern in beef post-rigor longissimus dorsi muscle were studied. The results showed that protein solubilization increased with increasing temperature, especially from 40 °C to 60 °C. A regular trend of protein solubilization was found when isolated myofibrils were subjected to high pressure at different temperatures, an increase was observed with increasing pressure up to about 400 MPa, solubility then decreasing to 600 MPa. Electrophoretic profiles showed that myosin light chains and actin thin filaments were sensitive to pressure, and were released from myofibrils subjected to 100 MPa and higher pressures at the different temperatures.

Show MeSH