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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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Changes in the concentration of myofibrillar protein in the supernatants obtained on centrifugation of the myofribillar extract after pressure treatment at (a) 20 °C, (b) 40 °C, and (c) 60 °C. 0.1 MPa is ambient pressure (control); a–e: means with different letters are significantly different (P < 0.05) between pressure treatments at a given processing temperature.
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f1-ijms-12-03034: Changes in the concentration of myofibrillar protein in the supernatants obtained on centrifugation of the myofribillar extract after pressure treatment at (a) 20 °C, (b) 40 °C, and (c) 60 °C. 0.1 MPa is ambient pressure (control); a–e: means with different letters are significantly different (P < 0.05) between pressure treatments at a given processing temperature.

Mentions: The effects of high pressure and temperature on the solubilization of myofibrillar proteins are presented in Figure 1.


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)

Changes in the concentration of myofibrillar protein in the supernatants obtained on centrifugation of the myofribillar extract after pressure treatment at (a) 20 °C, (b) 40 °C, and (c) 60 °C. 0.1 MPa is ambient pressure (control); a–e: means with different letters are significantly different (P < 0.05) between pressure treatments at a given processing temperature.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f1-ijms-12-03034: Changes in the concentration of myofibrillar protein in the supernatants obtained on centrifugation of the myofribillar extract after pressure treatment at (a) 20 °C, (b) 40 °C, and (c) 60 °C. 0.1 MPa is ambient pressure (control); a–e: means with different letters are significantly different (P < 0.05) between pressure treatments at a given processing temperature.
Mentions: The effects of high pressure and temperature on the solubilization of myofibrillar proteins are presented in Figure 1.

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