Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle.

Huff-Lonergan, Elisabeth J.; Mitsuhashi, Tomiko; Beekman, Dirk Douglas; Parrish, F. C.; Olson, D. G.; Robson, Richard M.

doi:10.2527/1996.745993x

Cited by 402 publications

(350 citation statements)

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“…For each temperature and pH decline combination, 2 myofibril populations were used. The pH decline of the digestions was monitored using a ThermoOrion PerpHect pH Meter, model 330 (Orion Research, Inc., Boston, MA), with pH measurements taken at 0, 0.17, 0.33, 0.5, 1, 3, 24, and 72 h. Myofibrils were digested by μ-calpain according to a modified procedure of Huff-Lonergan et al (1996a). Eight milliliters of glycerinated myofibrils were centrifuged at 3,100 × g for 6 min at 4°C and washed with 4 mL of 5 mM Tris-HCl (pH 8.0).…”

Section: Methodsmentioning

confidence: 99%

“…However, during storage, endogenous enzymes are able to decrease muscle tension as proteins are cleaved, weakening the structural integrity of muscle to improve meat tenderness in a process known as postmortem proteolysis (Aberle et al, 2001). This process is thought to primarily involve the calpain enzyme system (Koohmaraie, 1988;Huff-Lonergan et al, 1996a;Geesink et al, 2006;Mohrhauser et al, 2011); however, because prerigor postmortem temperature and pH conditions within muscle are not constant, optimal conditions for μ-calpain activity (25°C and pH of 6.5) are not always present within postmortem muscle (Boehm et al, 1998;Maddock et al, 2005). Additionally, it has been demonstrated that both pH and temperature can have dramatic effects on μ-calpain autolysis and activity.…”

Section: Methodsmentioning

confidence: 99%

“…Although it has been repeatedly reported that in vitro μ-calpain digestion of purified myofibrils can produce similar myofibrillar protein degradation patterns found in normal postmortem skeletal muscle (Koohmaraie et al, 1986;Koohmaraie, 1992;Huff-Lonergan et al, 1996a;Mohrhauser et al, 2011), conditions of these digestions have not mimicked the early temperature and pH conditions found in postmortem muscle due to many limitations. Therefore, most of the in vitro myofibrillar digestions by μ-calpain have occurred under constant pH and temperature conditions (Koohmaraie et al, 1986;HuffLonergan et al, 1996a;Weaver et al, 2009;Mohrhauser et al, 2011).…”

Section: Methodsmentioning

confidence: 99%

“…Numerous studies (Koohmaraie, 1988;Huff-Lonergan et al, 1996a;Geesink et al, 2006;Mohrhauser et al, 2011) provide compelling evidence that postmortem tenderization of beef is primarily modulated by the calpain protease system, specifically μ-calpain. These abundant enzymes have access to their substrates postmortem, require no ATP for activation, and have the ability to reproduce postmortem changes in vitro (Koohmaraie, 1988;Huff-Lonergan et al, 1996a). Despite this convincing evidence, it has been argued that calpains may lack the ability to function under normal postmortem temperature and pH conditions.…”

Section: Introductionmentioning

confidence: 99%

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Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline1

Mohrhauser

Lonergan

Huff-Lonergan

et al. 2014

Journal of Animal Science

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The objectives of this study were to 1) determine the conditions (temperature and pH) that exist in early postmortem muscle of normally chilled and delay chilled beef carcasses to provide a model for in vitro work and 2) determine the mechanism by which early postmortem temperature/pH conditions found in beef muscle influence the enzymes that regulate the aging process in vitro. For objective 1, 7 finished beef animals (HCW 385 ± 8 kg) were harvested with the right sides subjected to normal chilling (2.3°C) approximately 1.25 h postmortem and the left sides subjected to ambient temperature (delay chilling; 22.6°C) for an additional 4.75 h postmortem and then allowed to chill at 2.3°C. Delay chilled carcasses had a more rapid pH decline (P < 0.05) and a slower rate of carcass cooling (P < 0.05). No differences were observed between normally chilled and delay chilled samples for sarcomere length or postmortem proteolysis of troponin T (TnT; P > 0.10). Warner-Bratzler shear force (WBSF) was reduced in steaks from normally chilled carcasses at 14 d (P < 0.05), while results indicated a strong, positive correlation between 14-d WBSF and 3-h longissimus dorsi muscle (LM) temperature (r = 0.67, P < 0.01) as well as a strong, negative correlation between 14-d WBSF and 6-h LM pH (r = -0.65, P < 0.02). These results were used to design the methodology for objective 2, where isolated myofibrils were subjected to μ-calpain digestion at 4 or 22°C with either a fast or slow initial pH decline. As expected, digestions with a fast initial pH decline had lower pH values in the early time points of the incubation (P < 0.05). No differences were detected in μ-calpain activity or in the degradation of intact TnT between the fast and slow pH decline treatments (P > 0.10); however, warmer digestions resulted in a tendency for increased activation of μ-calpain (P < 0.10) and a significant reduction in intact TnT (P < 0.05). Additionally, a temperature × time interaction was revealed in μ-calpain activity and in the degradation of intact TnT (P < 0.05). Specifically, assayed calpain activity was lower at 0.17, 0.33, 1, and 3 h and greater at 72 h in warmer digestions, while intact TnT disappearance was greater as both time and digestion temperature increased. Meat aging and μ-calpain activity are influenced by both temperature and pH, but more research is necessary to fully realize their relationships. ABSTRACT: The objectives of this study were to 1) determine the conditions (temperature and pH) that exist in early postmortem muscle of normally chilled and delay chilled beef carcasses to provide a model for in vitro work and 2) determine the mechanism by which early postmortem temperature/pH conditions found in beef muscle influence the enzymes that regulate the aging process in vitro. For objective 1, 7 finished beef animals (HCW 385 ± 8 kg) were harvested with the right sides subjected to normal chilling (2.3°C) approximately 1.25 h postmortem and the left sides subjected to ambient temperature (delay chilling; 22.6°C) for a...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline1

Mohrhauser

Lonergan

Huff-Lonergan

et al. 2014

Journal of Animal Science

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“…Como exemplo podemos citar a desmina e a troponina T, que são degradadas durante o período de maturação da carne em refrigeração (HUFF-LONERGAN et al, 1996;TAYLOR et al, 1995;WHIPPLE et al, 1990 (CONTRERAS-CASTILLO et al, 2016;LOMIWES et al, 2013;PULFORD et al, 2009PULFORD et al, , 2008PURCHAS;YAN;HARTLEY, 1999;TONG;GIBSON, 1991).…”

Section: Introductionunclassified

Impacto do pH final na maciez do músculo <i>Longissimus lumborum </i>de animais zebuínos: mudanças estruturais de proteínas da carne crua e cozida durante a maturação

Mera¹

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DEDICATÓRIADedico este trabajo con amor, a mi familia, especialmente a mis padres e hermanos, personas que confiaron y creyeron en mí desde siempre. AGRADECIMENTOSAgradezco en primer lugar a Dios, por la vida, por colocarme en el camino correcto, por darme la suficiente fortaleza y sabiduria para hacer frente a las dificultades presentadas en mi vida. A Ti todo mi amor y mi vida.A mis queridos padres por darme la vida, y a mis hermanos, por todo el apoyo moral, nada hubiese conseguido sin ellos.A la Profesora Carmen, por la confianza que me brindó para realizar la maestría sin conocerme. Más que una orientadora, un amiga que admiro demasiado.A mis queridos amigos, mis hermanos de padres distintos, mi familia en el Brasil: Erick, Melina, Claudio, Carmen, Yemina y Rafael, muchas gracias por todo.Al Gobierno Peruano, sin duda logró una revolución en la Educación Superior, todo mi agradecimiento al Programa Nacional de Becas y Crédito EducativoPronabec, por la beca que me otorgaron.Al equipo del laboratorio de "Qualidade e Processamento de Carnes", por todo el apoyo en el desarrollo del experimento.Al equipo del "Laboratorio de Anatomia e Fisiologia Animal -LAFA", especialmente al Profesor Eduardo y a Giuliana, por birndarme el espacio y orientación en la realización de los análisis del experimento.A Pierre Delmorio, funcionario de Mettler-Toledo, por todo el apoyo en el análisis de DSC, fue pieza clave para la ejecución del experimento.Al profesor Gilberto José de Moraes, por brindarme el microscopio de contraste de fase para el análisis de "comprimento de sarcômero" A mi favela querida: Kathelyn, Miriam, Erick, Mariana, Beatriz, Bruna y Juan, muchas gracias por todos los momentos felices con ustedes.A la república "Casa Nova", muchas gracias por la conviviencia durante más de un año en el Brasil.A todos mis familiares y amigos que directa o indirectamente estuvieron apoyándome en el desarrollo de la maestría. RESUMO Impacto do pH final na maciez do músculo Longissimus lumborum de animais zebuínos: mudanças estruturais de proteínas da carne crua e cozida durante a maturaçãoO objetivo do presente trabalho foi determinar a força de cisalhamento Warner-Bratzler do músculo Longissimus lumborum de animais zebuínos machos inteiros (Bos indicus) durante o período de maturação, nas faixas de pH final (pHf 48 horas post mortem) normal (pH entre 5,5 e 5,8) e anormal (pH entre 5,81 e 6,19) e temperaturas internas de cozimento. Concomitante com a avaliação de força de cisalhamento, foram avaliadas também a degradação da desmina e troponina T, o comprimento do sarcômero, o teor de colágeno total e solúvel, as temperaturas máximas de desnaturação das proteínas e a morfologia geral de agregação das fibras do músculo no cozimento. A degradação da desmina e troponina T foi maior no pHf normal, aparecendo produtos de degradação a partir do dia 7 nessa faixa de pHf. Não houve diferenças nos valores de comprimento do sarcômero, descartandose assim, a contribuição desse parâmetro sobre a temperatura máxima de desnaturação (Tmáx) das...

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Effect of prerigor lactic acid treatment on lysosomal enzyme release in bovine muscle

Ertbjerg

Larsen

Møller

1999

J. Sci. Food Agric.

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Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle.

Cited by 402 publications

References 53 publications

Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline1

Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline1

Impacto do pH final na maciez do músculo <i>Longissimus lumborum </i>de animais zebuínos: mudanças estruturais de proteínas da carne crua e cozida durante a maturação

Effect of prerigor lactic acid treatment on lysosomal enzyme release in bovine muscle

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