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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 40 °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, 3 represent myosin light chains 1 and 3, respectively.
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f3-ijms-12-03034: SDS-PAGE profiles from supernatants (A) and precipitates (B) of myofibrils after pressure treatment at 40 °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, 3 represent myosin light chains 1 and 3, respectively.

Mentions: In the samples pressure treated at 40 °C and 60 °C, similar protein solubility changes were found (Figure 3 and Figure 4). New banding patterns were observed. Lower molecular weight bands (below 35 KDa) increased with the pressure up to 200 or 400 MPa in the supernatants, but there were no significant changes in the precipitates. These results are similar to those of Sikes et al. who found that when the myofibrillar proteins of beef neck were treated at 200 MPa and 60 °C for 20 min a new type of structure between myosin and actin was formed and the myofibrillar proteins degraded to smaller molecules [14]. In the present study the band with the molecular weight of about 18 KDa (LC2) disappeared in the samples pressure treated at 40 °C and 60 °C, presumably due to the interactive effect of pressure and temperature treatment.


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 40 °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, 3 represent myosin light chains 1 and 3, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f3-ijms-12-03034: SDS-PAGE profiles from supernatants (A) and precipitates (B) of myofibrils after pressure treatment at 40 °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, 3 represent myosin light chains 1 and 3, respectively.
Mentions: In the samples pressure treated at 40 °C and 60 °C, similar protein solubility changes were found (Figure 3 and Figure 4). New banding patterns were observed. Lower molecular weight bands (below 35 KDa) increased with the pressure up to 200 or 400 MPa in the supernatants, but there were no significant changes in the precipitates. These results are similar to those of Sikes et al. who found that when the myofibrillar proteins of beef neck were treated at 200 MPa and 60 °C for 20 min a new type of structure between myosin and actin was formed and the myofibrillar proteins degraded to smaller molecules [14]. In the present study the band with the molecular weight of about 18 KDa (LC2) disappeared in the samples pressure treated at 40 °C and 60 °C, presumably due to the interactive effect of pressure and temperature treatment.

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