Strategies to improve beef tenderness by activating calpain-2 earlier postmortem

Colle, M. J.; Nasados, J. A.; Rogers, J. M.; Kerby, D. M.; Buren, Jessie B Van; Richard, R.P.; Murdoch, Gordon K.; Williams, Christopher J.; Doumit, M. E.

doi:10.1016/j.meatsci.2017.08.008

Cited by 35 publications

(20 citation statements)

References 21 publications

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“…Geesink et al (2006) indicated that calpain-1 is mostly responsible for postmortem proteolysis, whereas Colle and Doumit (2017) reported that calpain-2 was activated in LL and semimembranosus steaks during extended aging (up to 42 d). Additionally, Colle et al (2018) reported calpain-2 can contribute to early proteolysis, but calcium chloride injection or freezing of the meat was required. The endogenous inhibitor of the calpains, calpastatin, can have a negative effect on the extent of postmortem proteolysis.…”

Section: Discussionmentioning

confidence: 99%

Effect of Brahman genetics on myofibrillar protein degradation, collagen crosslinking, and tenderness of the longissimus lumborum1

Phelps

Johnson

Elzo

et al. 2017

Journal of Animal Science

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The objective of this study was to examine the effect of percent Brahman genetics on Warner-Bratzler shear force (WBSF), desmin and troponin-T (TnT) degradation, hydroxylysyl pyridinoline (HP) crosslink content, and perimysial collagen melting temperature. Steers ( = 131) produced in 2012 and 2013 were harvested at 1.27 cm of visual s.c. back fat thickness. Steers were divided into 4 genetic categories consisting of steers that contained 6/32 or less Brahman genetics, 12/32 Brahman genetics, 14/32 to 18/32 Brahman genetics, and 23/32 to 32/32 Brahman genetics. Twenty-four hours after harvest, a 7.62-cm piece of the longissimus lumborum beginning at the 13th rib was collected and aged for 14 d. Following aging, three 2.54-cm steaks were cut for WBSF, trained sensory panel, and laboratory analyses. Laboratory analyses steaks were used to determine protein degradation, HP crosslink analysis, and perimysial collagen melting temperature. Data were analyzed using a polynomial regression for unequally spaced treatments. As the percent Brahman genetics increased, WBSF increased (linear, = 0.01). As percent Brahman genetics increased, tenderness score decreased (less tender) and connective tissue score increased (more connective tissue; linear, = 0.01). As the percentage of Brahman genetics increased, the amount of degraded desmin (38 kDa) and TnT (34 and 30 kDa) decreased (linear, < 0.03) whereas the amount of immunoreactive 36 kDa TnT increased (linear, = 0.04). Percent Brahman genetics had no effect ( = 0.14) on HP crosslink content but did tend to increase ( = 0.07) perimysial collagen melting temperature as the percent Brahman increased. The percentage of Brahman genetic influence was positively correlated to WBSF ( = 0.25), 36 kDa immunoreactive TnT ( = 0.26), and perimysial collagen melting temperature ( = 0.25, = 0.01). Sensory panel tenderness ( = -0.44), juiciness ( = -0.26), and connective tissue scores ( = -0.63); 38 kDa degraded desmin ( = -0.34), 34 ( = -0.36) and 30 kDa degraded TnT ( = -0.29); and HP collagen crosslinks ( = -0.20) were negatively correlated to percent Brahman genetic influence ( < 0.03). Increasing Brahman genetic influence in steers negatively affects tenderness, partially through a reduction in degradation of desmin and TnT. Although HP collagen crosslinks are unaffected by Brahman genetics, a tendency for increased perimysium melting temperature indicates that other collagen-stabilizing crosslinks may be affected.

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Section: Discussionmentioning

confidence: 99%

Effect of Brahman genetics on myofibrillar protein degradation, collagen crosslinking, and tenderness of the longissimus lumborum1

Phelps

Johnson

Elzo

et al. 2017

Journal of Animal Science

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“…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%

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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“…Previous research has showed that CAST have an important effect on tenderness. Meat quality and tenderness could be improved by activating calpain or reducing CAST activity (Colle et al, 2018). The CAST gene is an important marker for pork quality and carcass traits (Djurkin et al, 2016).…”

Section: The Relationship Between Gene Expression and Carcass Lean Imf Contentmentioning

confidence: 99%

The Differential Expressions of PPARγ and CAST mRNA in Muscle Tissues of Jinhua and Landrace Pigs

Zhao

Guo

Miao

et al. 2020

IJAR

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Background: Fat deposition affected meat quality and the suitable amount of intramuscular fat (IMF) can significantly improve the taste of meat, palatability, juicy, tenderness and flavor, thereby enhancing the meat quality in animals. Although, calpastatin (CAST) and peroxisome proliferator-activated receptor-ã (PPARã) could regulate meat quality by altering meat tenderness or IMF content in animals, reports concerning the relationship between CAST, PPARã expression and pork quality is unclear.Methods: A total of twenty 28-day-old purebred weaned Jinhua and Landrace piglets (10 piglets per breed) were divided into two groups according to breed for the feeding trials lasting for 120 days. At the 148 days of age, 3 pigs of each breed were selected to slaughter. Total RNA was extracted from longissimus dorsi and biceps femoris muscle to investigate the differential expression of PPARã and CAST in muscle tissues of different breed pigs by RT-PCR methods, as well as their relationship with IMF and carcass lean content.Result: These results suggested that PPARã is an important effector for regulating fat deposition in pigs, which was correlated with IMF and carcass lean content of pigs. This data would provide a scientific basis for the regulation of pork quality.

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Strategies to improve beef tenderness by activating calpain-2 earlier postmortem

Cited by 35 publications

References 21 publications

Effect of Brahman genetics on myofibrillar protein degradation, collagen crosslinking, and tenderness of the longissimus lumborum1

Effect of Brahman genetics on myofibrillar protein degradation, collagen crosslinking, and tenderness of the longissimus lumborum1

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

The Differential Expressions of PPARγ and CAST mRNA in Muscle Tissues of Jinhua and Landrace Pigs

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