Effects of Oxidation <i>in Vitro</i> on Structures and Functions of Myofibrillar Protein from Beef Muscles

Fu, Qingquan; Li, Rui; Hai-ou, Wang; Hu, Chun; Song, Shangxin; Zhou, Guanghong; Zhang, Wangang

doi:10.1021/acs.jafc.9b01239

Cited by 85 publications

(64 citation statements)

References 60 publications

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“…Furthermore, during the post-mortem period, endogenous proteases activity in the muscle are responsible to decrease the muscle quality (Qin et al, 2020). The role of calpain as an endogenous protease enzyme on myofibrillar proteins degradation in fish and beef muscles has been previously confirmed (Wang et al, 2011;Fu et al, 2019). Therefore, investigations on calpain activity during the post-mortem period can provide additional details about the role of this enzyme on protein degradation and also its activity in different muscle parts.…”

Section: Introductionmentioning

confidence: 98%

Comparison between lipid and protein oxidation progress in the tail and claw muscles of signal crayfish (Pacifastacus leniusculus)

Hematyar

Policar

Samarin

et al. 2020

Int J of Food Sci Tech

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Microbial activity and then oxidation progress are the most important freshness indicators during postmortem. In this study, we monitored proteomic and microbial changes, as well as biochemical degradation, in the tail and claw muscles of crayfish stored for 12 days at +4°C. One specified protein band at 107 kDa in the claw muscle and two specified protein bands in the tail muscle at 140 and 36-40 kDa were identified. Western blotting indicated a higher amount of oxidised proteins in the tail compared to the claw muscle. Tail muscle showed higher oxidation progress and calpain activity than claw one. Both muscles were spoiled after 12 days with respect to total viable counts. In the first days, calpain activity is the main reason for protein degradation, while protein oxidation dominates for the rest of the time. Lipid-protein oxidation progress showed probably, protein oxidation started earlier than lipid oxidation in both muscles.

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Section: Introductionmentioning

confidence: 98%

Comparison between lipid and protein oxidation progress in the tail and claw muscles of signal crayfish (Pacifastacus leniusculus)

Hematyar

Policar

Samarin

et al. 2020

Int J of Food Sci Tech

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“…Previous studies demonstrated that disulfide bonds are the primary covalent cross‐linking bonds responsible for aggregate formation (Xiong, Blanchard, Ooizumi, & Ma, 2010). A recent study identified oxidation sensitive sites in beef MPs by proteomics, suggesting that myosin, actin, calpains, and caspases are easily oxidized to form disulfide bonds due to their higher free sulfhydryl group content (Fu et al., 2019). The dityrosine bonds formation is correlated with protein sources.…”

Section: Oxidationmentioning

confidence: 99%

“…The structure of pork MPs is more easily altered at high ferric ion concentrations, and the pattern of changes is independent from the content of FeCl 3 (Park, Xiong, & Alderton, 2007). Different sources of MPs have been subjected to the Fenton system with various concentrations of H 2 O 2 and evaluated for covalent modification and their effects on gelation properties, including pork (Xia et al., 2019; Xiong et al., 2010), chicken (Liu & Xiong, 2015; Xia et al., 2018), beef (Fu et al., 2019), and fish (Li, Kong, Xia, Liu, & Diao, 2013; Lu, Zhang, Li, & Luo, 2017).…”

Section: Oxidationmentioning

confidence: 99%

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

Zhang

Zhou

2020

Comp Rev Food Sci Food Safe

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To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic–protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat‐induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose‐dependent and dual‐role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross‐linked three‐dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.

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“…In this sense, numerous studies have been conducted and demonstrated that a process with mild protein oxidation, at a very low oxidant concentration, for example, <1 mM H 2 O 2 , could enhance the gel properties of MP by changing the mode of myosin aggregation, which was ascribed to the shift of myosin cross‐linking in the early stage of heating from head–head association to prevalently tail–tail aggregation through disulfide bonds. While a process with excessive oxidation tended to cause larger protein aggregates, which were morphologically incapable of generating a fine gel network and instead generated a porous coagulum (Chanarat, Benjakul, & Xiong, 2015; Fu et al., 2019; Li, Li, Wang, Zhang, & Xie, 2014; Wang, He, Gan, & Li, 2018; Wang, Xiong, & Sato, 2017; Zhang et al., 2020). To elucidate the structure‐modifying effect of oxidation on the susceptibility of pork MP to MTG at 0.6 mol/L NaCl (equivalent to about 2% to 3% salt in processed meats), Li, Xiong, and Chen (2012) found that a mild oxidation process promoted the MTG‐mediated cross‐linking of MP, while a strong oxidation process inhibited the MTG effect.…”

Section: Modification Of Mpmentioning

confidence: 99%

Modification of myofibrillar protein functional properties prepared by various strategies: A comprehensive review

2020

Comp Rev Food Sci Food Safe

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Today, both consumers and food industry producers have exhibited an ever‐growing interest in improving and broadening the functional performance of proteins in food industry. Myofibrillar protein (MP) is mainly responsible for texture, yield and organoleptic characteristics of final meat products. To increase functional properties of MP, technological and nutritional improvement of MP is needed to modify its structure and functionalities. Considerable approaches, including additives, oxidation treatments, and novel food processing technologies, have been utilized to modify its functional properties to manufacture acceptable meat products with lower cost and more desirable nutritional characteristics. However, a comprehensive summary of structural and functional changes of MP in response to different modification strategies is still lacking. Hence, in this review paper, our main goal is first to provide an overview of the functional characteristics of MP. Then, this review will mainly discuss the current knowledge on the functional changes of MP caused by various modification methods and will present some examples of previous works and recent progress. Finally, future outlooks are presented to tailor the manufacture of functionality enhanced and value‐added muscle‐based products and enable modified MP can be applied as a novel meat ingredient in food industry.

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Effects of Oxidation in Vitro on Structures and Functions of Myofibrillar Protein from Beef Muscles

Cited by 85 publications

References 60 publications

Comparison between lipid and protein oxidation progress in the tail and claw muscles of signal crayfish (Pacifastacus leniusculus)

Comparison between lipid and protein oxidation progress in the tail and claw muscles of signal crayfish (Pacifastacus leniusculus)

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

Modification of myofibrillar protein functional properties prepared by various strategies: A comprehensive review

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