Effect of extended aging on calpain-1 and -2 activity in beef longissimus lumborum and semimembranosus muscles

Colle, M. J.; Doumit, M. E.

doi:10.1016/j.meatsci.2017.05.014

Cited by 41 publications

(31 citation statements)

References 23 publications

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“…A total of 30% and 31% decrease was observed in the average shear force value of Biceps femoris and Semimembranosus , respectively, during the entire period of aging. These results are in agreement with the findings of Colle and Doumit () who also observed a significant decrease in the shear force of beef muscles during aging. A total decline of 17% was observed in the shear force of Longissimus dorsi of culled dairy cows subjected to 7 days of aging (Bunmee, Jaturasitha, Kreuzer, & Wicke, ).…”

Section: Resultssupporting

confidence: 93%

“…Aging has been reported to improve the tenderness of beef Semimembranosus and Biceps femoris by several studies (Colle & Doumit, ; Colle et al, ). The calpain system, a family of endogenous calcium‐dependent cysteine proteases, is associated with meat tenderness during aging and is believed to regulate the rate and the extent of the postmortem degradation of certain myofibrillar proteins including troponin‐T, desmin, nebulin, titin, and filamin (Bhat, Morton, Mason, & Bekhit, ; Huff‐Lonergan, Zhang, & Lonergan, ; Koohmaraie & Geesink, ).…”

Section: Introductionmentioning

confidence: 98%

“…Considered as the key enzyme for meat tenderization, calpain 1 is believed to be largely responsible for early postmortem proteolysis and thus plays a significant role in tenderization during aging (Bhat et al, ; Geesink, Kuchay, Chishti, & Koohmaraie, ; Kemp, Sensky, Bardsley, Buttery, & Parr, ; Pomponio & Ertbjerg, ). Calpain 2 has also been reported to be active and makes a significant contribution to proteolysis during an extended postmortem aging (Colle & Doumit, ; Colle et al, ).…”

Section: Introductionmentioning

confidence: 99%

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Calpain activity, myofibrillar protein profile, and physicochemical properties of beef Semimembranosus and Biceps femoris from culled dairy cows during aging

Bhat

Morton

Mason

et al. 2018

J Food Process Preserv

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The present study was conducted to elucidate the changes in the calpain activity, protein profile, and physicochemical properties of cold‐boned muscles from culled dairy cows during aging. Semimembranosus and Biceps femoris were used as the study model and were vacuum packaged and stored for 14 days at 4 ± 1°C. The samples were analyzed for pH, shear force, myofibrillar fragmentation index (MFI), calpain activity, and myofibrillar protein profile (1D‐SDS‐PAGE). A significant (p < 0.05) effect of aging was observed on the pH, shear force, and MFI of both the muscles. Casein zymography results indicated the presence of intact and autolyzed forms of calpain 1 and calpain 2. An increase in autolysis of the calpains and proteolysis was observed in both the muscles during aging. Aging for two weeks was effective (p < 0.05) in reducing the shear force of both the muscles by 30%; however, the aged muscles were still excessively tough. Practical applications Information is seldom available in the literature about the effect of aging on the calpain activity of the muscles from older animals, such as culled dairy cows, and the subsequent tenderization of such muscles during aging. An analysis of the changes in the proteins and activity of calpains during aging gives us an understanding of the biological basis of the changes in the tenderness of muscles. Tenderness of beef is considerably determined by the activity of the calpains and the changes in the myofibrillar proteins during aging. The results of the present study should be useful to the meat industry for predicting the beef quality, particularly the tenderness of the muscles from culled dairy animals during the aging process. Aging alone was not effective in tenderizing the muscles and other tenderization interventions are required in conjunction with aging, such as nonthermal technologies, to reduce the extra toughness associated with the muscles of culled dairy animals.

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Section: Resultssupporting

confidence: 93%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Calpain activity, myofibrillar protein profile, and physicochemical properties of beef Semimembranosus and Biceps femoris from culled dairy cows during aging

Bhat

Morton

Mason

et al. 2018

J Food Process Preserv

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“…During the storage period, the evidence suggest that CAPN1 and CAST activities declined significantly, whereas CAPN2 activity remained stable (9,53,54). In a recent research, calpain-1 activity was detected up to 42 days of postmortem, and autolyzed calpain-1 up to 70 days post-mortem.…”

Section: El Nuevo Marcador Capn1 4751 Fue úTil En Poblaciones De Bovimentioning

confidence: 90%

“…Durante el período de maduración de la carne, se ha determinado que las actividades de CAPN1 y CAST disminuyeron significativamente, mientras que la actividad de CAPN2 permaneció estable (9,53,54). En una investigación reciente, se detectó actividad de la proteina calpaína 1 hasta 42 días pos mortem, y actividad de la proteína autolizada hasta 70 días post mortem.…”

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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Effect of Ultrasound and Calcium Chloride on the Ultrastructure and the Warner-Bratzler Shear Force Value of Beef Shank Muscle Fibers

Wan

Wang

et al. 2018

Food Biophysics

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Effect of extended aging on calpain-1 and -2 activity in beef longissimus lumborum and semimembranosus muscles

Cited by 41 publications

References 23 publications

Calpain activity, myofibrillar protein profile, and physicochemical properties of beef Semimembranosus and Biceps femoris from culled dairy cows during aging

Calpain activity, myofibrillar protein profile, and physicochemical properties of beef Semimembranosus and Biceps femoris from culled dairy cows during aging

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

Effect of Ultrasound and Calcium Chloride on the Ultrastructure and the Warner-Bratzler Shear Force Value of Beef Shank Muscle Fibers

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