Myofibrillar protein denaturation/oxidation in freezing-thawing impair the heat-induced gelation: Mechanisms and control technologies

Zhang, Yuemei; Bai, Genpeng; Wang, Jinpeng; Wang, Ying; Jin, Guofeng; Teng, Wendi; Geng, Fang; Cao, Jinxuan

doi:10.1016/j.tifs.2023.06.035

Cited by 42 publications

(5 citation statements)

References 177 publications

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“…Chemical forces maintain the conformational stability of MP gels, and are closely related to strength, water retention, water distribution, and other gel properties ( Zhang et al, 2023 ). Ionic and hydrogen bonds are weak intermolecular interactions and are easily destabilized by high temperatures, and therefore are not the primary chemical forces responsible for maintaining the stability of MP gels( Guan et al, 2023 ).…”

Section: Resultsmentioning

confidence: 99%

From amino acid analysis to improved gel properties: The role of dl-valine in Landaise goose myofibrillar protein

Yan,

Li,

Wang

et al. 2024

Food Chemistry: X

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Section: Resultsmentioning

confidence: 99%

From amino acid analysis to improved gel properties: The role of dl-valine in Landaise goose myofibrillar protein

Yan,

Li,

Wang

et al. 2024

Food Chemistry: X

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“…In addition to the classical methods of inhibiting protein oxidation described above, new techniques have emerged. For example, various new freeze–thaw techniques such as ultrasonic‐assisted freezing/thawing, electric field‐assisted freezing/thawing and high‐pressure‐assisted freezing/thawing can accelerate the freezing/thawing process and thus slow down the damage caused by denaturation and oxidation of myofibrillar proteins by inhibiting the growth of ice crystals (Zhang et al ., 2023). It has been shown that ultrahigh‐pressure technology can also inhibit lipid oxidation, protein oxidation and degradation in blackfish during cold storage and maintain fish flesh and myofibrillar protein structure (Liu et al ., 2022a), and furthermore, it has been shown in studies on cod that ultrahigh pressure can avoid quality deterioration and protein oxidation during heat treatment by increasing the content of soluble protein nitrogen (Zhang et al ., 2019).…”

Section: Control Of Protein Oxidation In Aquatic Productsmentioning

confidence: 99%

“…thus slow down the damage caused by denaturation and oxidation of myofibrillar proteins by inhibiting the growth of ice crystals (Zhang et al, 2023). It has been shown that ultrahigh-pressure technology can also inhibit lipid oxidation, protein oxidation and degradation in blackfish during cold storage and maintain fish flesh and myofibrillar protein structure (Liu et al, 2022a), and furthermore, it has been shown in studies on cod that ultrahigh pressure can avoid quality deterioration and protein oxidation during heat treatment by increasing the content of soluble protein nitrogen (Zhang et al, 2019).…”

Section: Other Regulation Measuresmentioning

confidence: 99%

Recent advances in the effects of protein oxidation on aquatic products quality: mechanism and regulation

Zhao

Simpson

et al. 2023

Int J of Food Sci Tech

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SummaryAquatic products are delicious and rich in high‐quality proteins, and thus have high‐food value and are popular among consumers; however, deterioration of their quality can easily occur when being stored and processed. Proteins, the main components of the muscle tissue of aquatic products, are closely related to the quality of aquatic products, and protein oxidation has become a research hotspot for studying the regulatory mechanisms of aquatic product quality changes. Protein oxidation is one of the main causes of quality deterioration of aquatic products, mainly because of protein cross‐linking and protein degradation caused by oxidation. Related studies have also shown that the changes in the electrostatic charge of proteins owing to oxidation are associated with the muscle water‐holding capacity (WHC). This article introduces the induction mechanism of protein oxidation in aquatic products, focusing on its effects on the quality, such as colour, texture, WHC and summarises the current research progress of aquatic products quality control on this basis to provide theoretical reference for future research.

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“…However, during freeze–thaw processing, myofibrillar proteins are unavoidably denatured and oxidized as a result of the formation of ice crystals, which can result in excessive aggregation of myosin molecules with gel-like properties and prevent the formation of an excellent gel network during subsequent thermal processing (Figure ). , This suggests that the juiciness and organoleptic properties of gel-type muscle food are not adequately maintained. , …”

Section: Impact Of Ice On the Quality Of Muscle Foodmentioning

confidence: 99%

Coexisting with Ice Crystals: Cryogenic Preservation of Muscle Food─Mechanisms, Challenges, and Cutting-Edge Strategies

Xie,

Zhou,

Tan

et al. 2023

J. Agric. Food Chem.

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Cryopreservation, one of the most effective preservation methods, is essential for maintaining the safety and quality of food. However, there is no denying the fact that the quality of muscle food deteriorates as a result of the unavoidable production of ice. Advancements in cryoregulatory materials and techniques have effectively mitigated the adverse impacts of ice, thereby enhancing the standard of freezing preservation. The first part of this overview explains how ice forms, including the theoretical foundations of nucleation, growth, and recrystallization as well as the key influencing factors that affect each process. Subsequently, the impact of ice formation on the eating quality and nutritional value of muscle food is delineated. A systematic explanation of cutting-edge strategies based on nucleation intervention, growth control, and recrystallization inhibition is offered. These methods include antifreeze proteins, ice-nucleating proteins, antifreeze peptides, natural deep eutectic solvents, polysaccharides, amino acids, and their derivatives. Furthermore, advanced physical techniques such as electrostatic fields, magnetic fields, acoustic fields, liquid nitrogen, and supercooling preservation techniques are expounded upon, which effectively hinder the formation of ice crystals during cryopreservation. The paper outlines the difficulties and potential directions in ice inhibition for effective cryopreservation.

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Myofibrillar protein denaturation/oxidation in freezing-thawing impair the heat-induced gelation: Mechanisms and control technologies

Cited by 42 publications

References 177 publications

From amino acid analysis to improved gel properties: The role of dl-valine in Landaise goose myofibrillar protein

From amino acid analysis to improved gel properties: The role of dl-valine in Landaise goose myofibrillar protein

Recent advances in the effects of protein oxidation on aquatic products quality: mechanism and regulation

Coexisting with Ice Crystals: Cryogenic Preservation of Muscle Food─Mechanisms, Challenges, and Cutting-Edge Strategies

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