Caspase-3 does not enhance in vitro bovine myofibril degradation by Μu-calpain

Mohrhauser, D. A.; Kern, Sandra; Underwood, K. R.; Weaver, Amanda

doi:10.1016/j.meatsci.2013.07.098

Cited by 3 publications

(2 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Meat tenderness is the result of different factors such as the amount and solubility of connective tissue, sarcomere shortening during rigor development, and post mortem proteolysis of myofibrillar proteins. Their impact on tenderness depends on the muscle, its structure and composition (Mohrhauser, Kern, Underwood, & Weaver, ).…”

Section: Introductionmentioning

confidence: 99%

The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

Onopiuk

Półtorak

Wierzbicka

2018

J Food Process Preserv

View full text Add to dashboard Cite

The impact of muscle and aging time on meat tenderness in carcasses of Limousin × Holstein‐Friesian bulls was evaluated. The scope of the research covered measurement of pH, basic composition, total collagen, shear force (WBSF), myofibrillar fragmentation index (MFI), and analysis of proteins with the use of SDS‐PAGE electrophoresis. The results underline the strong relationship between the chemical composition and collagen content of meat and its tenderness. The MFI as an index of advancement of the myofibrillar degradation process showed a high correlation with the instrumentally estimated shear force. In all muscles, a decrease of desmin, troponin T (TnT) and an increase of TnT derived polypeptides during aging were observed. The highest decrease of TnT together with the decrease WBSF in Semitendinosus (ST) muscles during aging resulted from a more extensive proteolysis in this muscle. The results indicate the relationship between the activity of selected proteins and the shear force, which may lead to a more effective prediction of meat tenderness. Practical applications Beef aging is an important process of preparing beef for consumption. Based on the results presented in this paper one may state that the phenomenon of bovine meat (Limousin × Holstein‐Friesian crossbred bulls) tenderness during post mortem aging is considerably related to the quality and quantity scope of changes on myofibrall proteins, mainly desmin, troponin T and proteins with molecular weight of 32‐27 kDa. The obtained results proved that meat tenderness and proteolytic changes during aging are related to the type of muscle, its function and location in the carcass. The results show a strong relationship between the activity of selected proteins and shear force value, which confirms by high correlation coefficients. Analysis of muscle proteins during aging is necessary to understand the biological basis of changes in meat tenderness and their differences among muscles. The information available in the current study should be very useful to the meat industry for prediction of beef quality especially beef tenderness during the aging process.

show abstract

Section: Introductionmentioning

confidence: 99%

The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

Onopiuk

Półtorak

Wierzbicka

2018

J Food Process Preserv

View full text Add to dashboard Cite

show abstract

“…Through electrophoretic separation of proteins and the identification using western blot method, it was possible to show the difference in the activity of the calpain system at 2, 4, 6, 24, and 48 hr postmortem. In addition, pH and temperature during the postslaughter chilling also have effects on the activity of calpains, as a reduction in pH or temperature would lower the activity (Mohrhauser, Kern, Underwood, & Weaver, ). Figure presents the changes in the activity of the calpain system.…”

Section: Resultsmentioning

confidence: 99%

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

Onopiuk

Półtorak

Sun

et al. 2017

J Food Process Engineering

View full text Add to dashboard Cite

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.

show abstract

Degradation and evaluation of myofibril proteins induced by endogenous protease in aquatic products during storage: a review

Qian

Chu

2023

Food Sci Biotechnol

View full text Add to dashboard Cite

Caspase-3 does not enhance in vitro bovine myofibril degradation by Μu-calpain

Cited by 3 publications

References 0 publications

The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

The impact of muscle and aging time on meat tenderness in the carcasses of Limousin × Holstein-Friesian crossbred bulls

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

Degradation and evaluation of myofibril proteins induced by endogenous protease in aquatic products during storage: a review

Contact Info

Product

Resources

About