Prediction of troponin-T degradation using color image texture features in 10d aged beef longissimus steaks

Sun, Xiaorui; Chen, K.J.; Berg, E. P.; Newman, David J.; Schwartz, Carlos; Keller, W.L.; Carlin, K.R. Maddock

doi:10.1016/j.meatsci.2013.09.012

Cited by 22 publications

(9 citation statements)

References 27 publications

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“…By electrophoretic separation of muscle proteins and the use of monoclonal antibodies for specifically tracking troponin T, it was proved that troponin T significantly decreased with aging time ( p < .001), as presented in Table . The results obtained concur with earlier studies by Sun et al () and Moczkowska, Półtorak, and Wierzbicka (). The most significant drop in the level of troponin T occurred in both ST and PM from the 2nd to 7th days of aging, when the activity decreased by 17.30 and 20.42%, respectively.…”

Section: Resultssupporting

confidence: 93%

Section: Impact Of Troponin T Degradation On Shear Forcesupporting

confidence: 93%

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Effects of selected myofibrillar protein activities on beef tenderization process based on electrophoretic analysis

Onopiuk

Półtorak

Sun

et al. 2017

J Food Process Engineering

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Meat aging process involves in changes in the microstructure of muscle fibers and calpains (cysteine endopeptidase) are responsible for this process, as calpains have direct access to myofibrils in a cell. The electrophoretic analysis (SDS–PAGE) presented in the current study aimed at investigating the impact of calpain system and troponin T on the changes in the Warner–Bratzler shear force in selected semitendinosus (ST) and psoas major (PM) muscles taken from 9 Holstein Frisian × Limousin crossbreed carcasses aged 25 ± 1 months. The presence of calpains, calpastatin, and troponin T was verified based on the western blot method using monoclonal antibodies for tracing specific proteins. The results also confirmed significant correlations between the amount of µ‐ and m‐calpains and troponin T degradation products and the shear force values and thus the tenderization process during beef aging. Practical applications Beef aging is an important process of preparing beef for consumption. During aging, the increase in the tenderness is affected by the changes in troponin T. The measurement of the amount of this protein can be an indicator of the changes of hardness during aging. The current results indicated that the tenderness of beef increased when the beef contained a greater amount of 30 kDa protein product and when the muscles had longer sarcomeres. The information available in the current study should be very useful to the meat industry for early prediction of beef quality especially beef tenderness during the aging process.

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Section: Resultssupporting

confidence: 93%

Section: Impact Of Troponin T Degradation On Shear Forcesupporting

confidence: 93%

Effects of selected myofibrillar protein activities on beef tenderization process based on electrophoretic analysis

Onopiuk

Półtorak

Sun

et al. 2017

J Food Process Engineering

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show abstract

“…2). Troponin-T forms a complex with tropomyosin and its degradation has been used as a marker of myofibrillar protein degradation in aged beef (Sun et al, 2014). Increased proteolysis of troponin-T has been shown to be promoted under various tenderisation treatments (Claeys, Smet, Balcaen, Raes, & Demeyer, 2004;Han et al, 2009;Ho et al, 1994;McBride & Parrish, 1977) and significantly correlated to shear force values (Marino et al, 2013).…”

Section: Effects Of Pef Treatment On Post-mortem Proteolysis Of Cold-mentioning

confidence: 99%

Effect of pulsed electric field on the proteolysis of cold boned beef M. Longissimus lumborum and M. Semimembranosus

et al. 2015

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“…All the PEF treated samples, had more troponin-T proteolysis compared with control samples at 21 day post-treatment time with bands in the 5 kV-20 Hz and 10 kV-20 Hz samples being the most prominent. The degradation of troponin-T has been widely used as an indication of myofibrillar protein degradation during ageing (Sun et al, 2014). Therefore, an increase in troponin-T proteolysis has been associated with an increase in tenderisation of beef muscles (Claeys, Smet, Balcaen, Raes, & Demeyer, 2004;Han et al, 2009;Ho et al, 1994;McBride & Parrish, 1977) and significantly correlates to shear force values (Marino et al, 2013).…”

Section: Effects Of Pef Treatment On Post-mortem Proteolysis Of Hot-bmentioning

confidence: 99%

Effect of pulsed electric field treatment on hot-boned muscles of different potential tenderness

et al. 2015

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Prediction of troponin-T degradation using color image texture features in 10d aged beef longissimus steaks

Cited by 22 publications

References 27 publications

Effects of selected myofibrillar protein activities on beef tenderization process based on electrophoretic analysis

Effects of selected myofibrillar protein activities on beef tenderization process based on electrophoretic analysis

Effect of pulsed electric field on the proteolysis of cold boned beef M. Longissimus lumborum and M. Semimembranosus

Effect of pulsed electric field treatment on hot-boned muscles of different potential tenderness

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