Postmortem proteolysis in three muscles from growing and mature beef cattle

Cruzen, Shannon M.; Paulino, Pedro Veiga Rodrigues; Lonergan, Steven M.; Huff-Lonergan, Elisabeth J.

doi:10.1016/j.meatsci.2013.09.021

Cited by 61 publications

(47 citation statements)

References 63 publications

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“…These findings are in agreement with our results, because Nellore muscle showed greater abundance of TPM1 and TNNT3 compared to Angus. Tropomyosin (Tpm) and troponin T (TnT) are among the main substrates of the proteolytic enzymes related to meat tenderization [23], and TnT degradation during aging has been positively associated with beef tenderization [17, 24]. …”

Section: Resultsmentioning

confidence: 99%

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

et al. 2017

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Proteins are the major constituents of muscle and are key molecules regulating the metabolic changes during conversion of muscle to meat. Brazil is one of the largest exporters of beef and most Brazilian cattle are composed by zebu (Nellore) genotype. Bos indicus beef is generally leaner and tougher than Bos taurus such as Angus. The aim of this study was to compare the muscle proteomic and phosphoproteomic profile of Angus and Nellore. Seven animals of each breed previously subjected the same growth management were confined for 84 days. Proteins were extracted from Longissimus lumborum samples collected immediately after slaughter and separated by two-dimensional electrophoresis. Pro-Q Diamond stain was used in phosphoproteomics. Proteins identification was performed using matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Tropomyosin alpha-1 chain, troponin-T, myosin light chain-1 fragment, cytoplasmic malate dehydrogenase, alpha-enolase and 78 kDa glucose-regulated protein were more abundant in Nellore, while myosin light chain 3, prohibitin, mitochondrial stress-70 protein and heat shock 70 kDa protein 6 were more abundant in Angus (P<0.05). Nellore had higher phosphorylation of myosin regulatory light chain-2, alpha actin-1, triosephosphate isomerase and 14-3-3 protein epsilon. However, Angus had greater phosphorylation of phosphoglucomutase-1 and troponin-T (P<0.05). Therefore, proteins involved in contraction and muscle organization, myofilaments expressed in fast or slow-twitch fibers and heat shock proteins localized in mitochondria or sarcoplasmic reticulum and involved in cell flux of calcium and apoptosis might be associated with differences in beef quality between Angus and Nellore. Furthermore, prohibitin appears to be a potential biomarker of intramuscular fat in cattle. Additionally, differences in phosphorylation of myofilaments and glycolytic enzymes could be involved with differences in muscle contraction force, susceptibility to calpain, apoptosis and postmortem glycolysis, which might also be related to differences in beef quality among Angus and Nellore.

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Section: Resultsmentioning

confidence: 99%

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

et al. 2017

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“…Calpastatin activity in muscle from older animals is more persistent postmortem than in muscle from growing animals (58). This difference may contribute to decreased protein degradation and increased toughness of beef from mature cattle, even after aging.…”

Section: Cuantificación Y Actividad De Proteínasmentioning

confidence: 98%

“…Muscle type, fiber type, gender, age and feeding strategies can influence calpain and calpastatin expression and/or activities. Muscle conversion involves La actividad de la calpastatina en el músculo de animales de mayor edad es más persistente post mortem que en el músculo de animales en crecimiento (58). Esta diferencia puede contribuir a la disminución de la degradación de las proteínas y al aumento de la dureza de la carne bovina, incluso después de la maduración.…”

Section: Cuantificación Y Actividad De Proteínasunclassified

El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.

2018

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Tenderness is considered the most important meat quality trait regarding its eating quality. Post mortem meat tenderization is primarily the result of calpain mediated degradation of key proteins within muscles fibers. The calpain system originally comprised three molecules: two Ca 2+ -dependent proteases and a specific inhibitor. Numerous studies have shown that the calpain system plays a central role in postmortem proteolysis and meat tenderization. The objective of this review is to describe the last biochemical and molecular findings in connection with this proteolytic system and their relation with meat tenderness in bovine. Findings of DNA polymorphisms and mRNA and protein expression are described as tools to predict meat tenderness. Understanding the molecular basis of meat tenderization may be useful particularly to the meat industry and may allow amendment of pre-slaughter handling practices and postmortem treatments that improves meat quality.Keywords: Bovine, Molecular Markers, Tenderness (Source: AGROVOC). RESUMENLa terneza de la carne es considerada como el atributo de mayor importancia en el concepto de calidad de carne. El proceso de tenderización de la carne post mortem es principalmente el resultado de la degradación de proteínas clave de las fibras musculares, mediado por las proteasas del sistema calpaína. Este sistema proteico está compuesto por tres moléculas: dos proteasas calcio-dependientes y su inhibidor específico. Numerosos estudios han demostrado que el sistema calpaína desempeña un papel central en la proteólisis postmortem y en la tenderización de la carne. El objetivo de esta revisión es describir los últimos descubrimientos bioquímicos y moleculares de este sistema proteolítico y su relación con la terneza de la carne bovina. Se describen los hallazgos de polimorfismos de ADN y de expresión de ARNm y proteínas, como herramientas para predecir la terneza de la carne. La comprensión de las bases moleculares de la tenderización de la carne puede ser de utilidad para la industria cárnica, permitiendo la modificación de las prácticas de manipulación antes del sacrificio y los tratamientos post mortem, mejorando la calidad de la carne bovina.

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“…The other explanation may involve the calpain/calpastatin system, related to the changes of post-mortem muscle fibres proteolysis. According to Cruzen et al, (2014) the ratio of calpain to calpastatin is lower in the old animals compared to the calves, indicating the reduced potential for proteolysis in the mature cattle.…”

Section: Effect Of Age On Colour Tenderness and Sensory Parameters Omentioning

confidence: 99%

Meat quality of Limousin young bulls slaughtered at 6, 9 and 12 months of age

et al. 2017

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The aim of this study was to compare the quality of meat of the young Limousin bulls slaughtered at the age of 6, 9 and 12 months, with particular regard to the residual glycogen content in the meat and the value of the glycolytic potential. The study was conducted on bovine longissimus lumborum muscle. The residual glycogen content, glycolytic potential value (96 h post-mortem), pH value (45 min, 24 h, 48 h and 96 h post-mortem), IMP/ATP index (45 min post-mortem), colour parameters (L*, a* and b*), natural and cooking losses, free water content, the chemical composition, sensory parameters (aroma, flavour, juiciness and tenderness) as well as instrumental tenderness based on cutting test (96 h post-mortem) were analysed. The slaughter age of bulls had significant (p<0.05) effect on following meat parameters: concentration of glycogen, glycolytic potential value, lightness (L*) and redness (a*), shear force value, intramuscular fat content and sensory evaluation of aroma, flavour, juiciness and tenderness. The longissimus lumborum muscle from young bulls slaughtered at the age of 6 months had significantly (p<0.05) lower values for glycogen concentration, glycolytic potential and intramuscular fat content when compared to animals slaughtered at the age of 12 months. Moreover, the colour of the examined muscle from the youngest bulls was characterised by the highest L* value and the lowest a* value as well as the lowest shear force value when compared to the meat of older bulls slaughtered at the age of 9 and 12 months.

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Postmortem proteolysis in three muscles from growing and mature beef cattle

Cited by 61 publications

References 63 publications

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

El sistema proteolítico calpaina en la tenderización de la carne: Un enfoque molecular.

Meat quality of Limousin young bulls slaughtered at 6, 9 and 12 months of age

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