Effect of pre-rigor temperature incubation on sarcoplasmic protein solubility, calpain activity and meat properties in porcine muscle

Liu, Jiao; Ruusunen, Marita; Puolanne, Eero; Ertbjerg, Per

doi:10.1016/j.lwt.2013.10.001

Cited by 44 publications

(28 citation statements)

References 28 publications

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“…The myofibrillar and sarcoplasmic proteins were extracted following the procedure described by Liu et al (2014) with slight modifications. Briefly, one gram (in duplicate) of frozen P. major muscle was homogenized by Ultra-Turrax (IKA, Germany) (30 s at 13,000 rpm, in ice) in 20 mL of cold Rigor Buffer (75 mM KCl, 10 mM KH 2 PO 4 , 2 mM MgCl 2 , 2 mM EGTA; pH 7.0) (Sigma-Aldrich, St. Louis, MO, United States).…”

Section: Sds-page Analysismentioning

confidence: 99%

Distribution and Expression of Vimentin and Desmin in Broiler Pectoralis major Affected by the Growth-Related Muscular Abnormalities

et al. 2020

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Desmin (DES) and Vimentin (VIM) exert an essential role in maintaining muscle cytoarchitecture and since are considered reliable markers for muscle regeneration, their expression has been extensively investigated in dystrophic muscles. Thus, exhibiting features similar to those of human dystrophic muscles, the present study aimed at assessing the distribution of VIM and DES proteins and the expression of the corresponding genes in Pectoralis major muscles affected by white striping (WS), wooden breast (WB), and spaghetti meat (SM) abnormalities as well as in those having macroscopically normal appearance (NORM). For this purpose, 20 Pectoralis major muscles (5/group) were collected from the same flock of fast-growing broilers to perform immunohistochemistry, immunoblotting and gene expression. Immunohistochemical analyses showed an increased number of fibers immunoreactive to both VIM and DES in WS and WB, while only a few immunoreactive fibers were observed in NORM. Concerning the protein level, if compared with NORM, a 55% increase in VIM content was found in WB affected cases (P < 0.05) thus suggesting the development of intense regenerative processes in an early-stage within these muscles. The significantly higher amount of DES (+53%) found in WS might be attributed to a progression of the regenerative processes that require its synthesis to preserve the structural organization of the developing fibers. On the other hand, significantly lower VIM and DES contents were found in SM. About gene expression, VIM mRNA levels gradually increased from the NORM to the SM group, with significantly higher gene expressions in WB and SM samples compared to the NORM group (P = 0.009 for WB vs. NORM and P = 0.004 for SM vs. NORM). Similarly, the expression of DES gene showed an increase from the NORM to WB group (P = 0.05). Overall, the findings of the present study suggest that intense regenerative processes take place in both WB and WS muscles although a different progression of regeneration might be hypothesized. On the other hand, the lack of correspondence between VIM gene expression and its protein product observed in SM suggests that VIM may also exert a role in the development of the SM phenotype.

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Section: Sds-page Analysismentioning

confidence: 99%

Distribution and Expression of Vimentin and Desmin in Broiler Pectoralis major Affected by the Growth-Related Muscular Abnormalities

et al. 2020

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“…Both a pH decline and ionic strength increase can lead to an increase in the hydrophobicity and aggregation of calpains, thereby decreasing their proteolytic activity against myofibrillar proteins (Huff- Lonergan & Lonergan, 2005). The prerigor high temperature incubation period induced an early activation of μ-calpain, resulting in tender postmortem meat (Hwang & Thompson, 2001;Liu, Ruusunen, Puolanne, & Ertbjerg, 2014). Oxidation or nitrosylation also affects calpain autolysis (see detailed review below).…”

Section: Proteolytic Systemmentioning

confidence: 99%

Stress Effects on Meat Quality: A Mechanistic Perspective

Xing

Gao

Tume

et al. 2018

Comp Rev Food Sci Food Safe

156

121

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Stress inevitably occurs from the farm to abattoir in modern livestock husbandry. The effects of stress on the behavioral and physiological status and ultimate meat quality have been well documented. However, reports on the mechanism of stress effects on physiological and biochemical changes and their consequent effects on meat quality attributes have been somewhat disjointed and limited. Furthermore, the causes of variability in meat quality traits among different animal species, muscle fibers within an animal, and even positions within a piece of meat in response to stress are still not entirely clear. This review 1st summarizes the primary stress factors, including heat stress, preslaughter handling stress, oxidative stress, and other stress factors affecting animal welfare; carcass quality; and eating quality. This review further delineates potential stress‐induced pathways or mediators, including AMP‐activated protein kinase‐mediated energy metabolism, crosstalk among calcium signaling pathways and reactive oxygen species, protein modification, apoptosis, calpain and cathepsin proteolytic systems, and heat shock proteins that exert effects that cause biochemical changes during the early postmortem period and affect the subsequent meat quality. To obtain meat of high quality, further studies are needed to unravel the intricate mechanisms involving the aforementioned signaling pathways or mediators and their crosstalk.

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“…Frozen minced meat was thawed at 5 °C overnight. The extraction of MP was conducted as described by Liu, Ruusunen, Puolanne, and Ertbjerg (2014) with some modification. Minced meat (200 g) was homogenized by IKA Ultra-Turrax T25 homogenizer (Labortechnik, Staufen, Germany) at 13,500 rpm for 2 min in 7 volumes of cold rigor buffer (75 mM KCl, 10 mM potassium phosphate, 2 mM MgCl2, 2 mM EGTA, pH 7.0).…”

Section: Preparation Of Mpmentioning

confidence: 99%

Myofibrillar protein gel properties are influenced by oxygen concentration in modified atmosphere packaged minced beef

Wang

Ertbjerg

2017

Food Chemistry

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Minced beef was stored for 8days and myofibrillar protein (MP) was extracted to investigate the effect of oxygen concentration (0, 20, 40, 60, and 80%) in modified atmosphere packaging (MAP) on heat-induced gel properties. Compression force of gels was lower when prepared from beef packaged in 0% oxygen, intermediate in 20 to 60% oxygen and greater in 80% oxygen. Total water loss of gels prepared from beef packaged with oxygen (20-80%) was higher and rheology measurements presented higher G' and G″ values. Additionally, gels from beef packaged without oxygen exhibited higher J (t) values during creep and recovery tests, demonstrating that oxygen exposure of meat during storage in MAP affect MP in such a way that heat-induced protein gels alter their characteristics. Generally, storage with oxygen in MAP resulted in stronger and more elastic MP gels, which was observed already at a relative low oxygen concentration of 20%.

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Effect of pre-rigor temperature incubation on sarcoplasmic protein solubility, calpain activity and meat properties in porcine muscle

Cited by 44 publications

References 28 publications

Distribution and Expression of Vimentin and Desmin in Broiler Pectoralis major Affected by the Growth-Related Muscular Abnormalities

Distribution and Expression of Vimentin and Desmin in Broiler Pectoralis major Affected by the Growth-Related Muscular Abnormalities

Stress Effects on Meat Quality: A Mechanistic Perspective

Myofibrillar protein gel properties are influenced by oxygen concentration in modified atmosphere packaged minced beef

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