Effect of inhibition of <i>μ</i>‐calpain on the myofibril structure and myofibrillar protein degradation in postmortem ovine muscle

Li, Zheng; Li, Xin; Gao, Xing; Du, Ming; Zhang, Dequan

doi:10.1002/jsfa.8018

Cited by 25 publications

(10 citation statements)

References 34 publications

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“…The color stability of meat with normal energy metabolism rate is good and the abnormal energy metabolism rate leads to development of PSE, DFD, and other defected meat (Hopkins et al., 2015; Ijaz et al., 2020). Changes in the structure and function of skeletal and myofibrillar proteins in lamb with abnormal energy metabolism result in dry or softened meat (Li, Li, Gao, Du, & Zhang, 2017). In the lamb with fast energy metabolism rate, the pH decline rate was increased, which led to the degeneration of muscle fiber structural proteins and the increase of fluid losses (Wang, He, et al., 2016).…”

Section: Protein Phosphorylationmentioning

confidence: 99%

Effects of protein posttranslational modifications on meat quality: A review

Zhang

Ren

et al. 2020

Comp Rev Food Sci Food Safe

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Meat quality plays an important role in the purchase decision of consumers, affecting producers and retailers. The formation mechanisms determining meat quality are intricate, as several endogenous and exogenous factors contribute during antemortem and postmortem periods. Abundant research has been performed on meat quality; however, unexpected variation in meat quality remains an issue in the meat industry. Protein posttranslational modifications (PTMs) regulate structures and functions of proteins in living tissues, and recent reports confirmed their importance in meat quality. The objective of this review was to provide a summary of the research on the effects of PTMs on meat quality. The effects of four common PTMs, namely, protein phosphorylation, acetylation, S‐nitrosylation, and ubiquitination, on meat quality were discussed, with emphasis on the effects of protein phosphorylation on meat tenderness, color, and water holding capacity. The mechanisms and factors that may affect the function of protein phosphorylation are also discussed. The current research confirms that meat quality traits are regulated by multiple PTMs. Cross talk between different PTMs and interactions of PTMs with postmortem biochemical processes need to be explored to improve our understanding on factors affecting meat quality.

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Section: Protein Phosphorylationmentioning

confidence: 99%

Effects of protein posttranslational modifications on meat quality: A review

Zhang

Ren

et al. 2020

Comp Rev Food Sci Food Safe

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“…К ним относятся белки теплового шока или шапероны и ферменты, участвующие в метаболизме [27]. Существует также сильная корреляция нежности с белками, которые защищают от окисления [28], и известно, что кальпаин очень восприимчив к окислению [29]. На активность протеаз также может влиять посттрансляционная модификация.…”

Section: кальпаиныunclassified

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2020

MIJ

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“…Troponin-T is located near actin and important for regulating actin-myosin interaction and maintaining the strength of thin filament (Yang et al, 2019). It is reported that troponin-T is cleaved by calpains (m/mcalpain), present in the sarcoplasm, and also by the lysosomal protease cathepsin B and L (de Oliveira et al, 2019;Li et al, 2017). Calpains are active at early stages, while the action of cathepsin B is related to the degree of postmortem lysosomal membrane breakdown, which occurs due to permeabilisation of the lysosomal membrane related to depletion of ATP reserves and malfunctioning of ionic pumps (Campus et al, 2010).…”

Section: Protein Denaturation and Degradationmentioning

confidence: 99%

Quality changes in high pressure processed tan mutton during storage

Peng

Tao

et al. 2020

Food sci. technol. int.

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The current study investigated the effects of high pressure (HP) treatment at 200 MPa and 500 MPa on quality characteristics of post-rigor tan mutton stored for 7 days at 4 °C, and textural changes were monitored during storage by means of the stress relaxation test. Application of 500 MPa high pressure significantly increased the elasticity and stiffness of meat after 7 days of storage ( P < 0.05), accompanied by a lighter and less red appearance and markedly enhanced centrifugal loss during storage campared to untreated ( P < 0.05). High pressure treatment at 200 MPa also substantially increased the lightness of samples throughout storage ( P < 0.05), and showed a significant increase in stiffness at the end of storage ( P < 0.05). Immunoblotting and electrophoresis (SDS-PAGE) analysis of key structural proteins revealed that myosin heavy chain denaturation began at 200 MPa, while actin denaturation occurred at 500 MPa. Troponin-T was continuously degraded in different treatments as storage progressed, and 200 MPa treatment and untreated represented similar degradation patterns, while 500 MPa treatment displayed more intense intact troponin-T at 38 kDa degradation. Results suggest that HP induced changes in cytoskeleton proteins, thereby affecting texture, water holding properties and lightness.

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Effect of inhibition of μ‐calpain on the myofibril structure and myofibrillar protein degradation in postmortem ovine muscle

Cited by 25 publications

References 34 publications

Effects of protein posttranslational modifications on meat quality: A review

Effects of protein posttranslational modifications on meat quality: A review

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Quality changes in high pressure processed tan mutton during storage

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