Concentration-dependent effect of eugenol on porcine myofibrillar protein gel formation

Chen, Hongsheng; Ma, Jinming; Pan, Deyin; Diao, Jiang; Guo, Anqi; Li, Runnan; Xiong, Youling L.

doi:10.1016/j.meatsci.2023.109187

Cited by 12 publications

(4 citation statements)

References 52 publications

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“…Recent studies have focused more on controlling protein oxidation by adding polyphenols and exploring how these additives influence the properties of myofibrillar fibrous protein gels [6,7]. The main reason is that the interaction between polyphenols and myofibrillar fibrous protein affects the amino acid side-chains of the protein, inducing changes in its secondary and tertiary conformations, which in turn alter its functional properties, especially its gelation properties [8]. Gnaphalium affine, a traditional wild vegetable commonly featured during the Qingming festival held in China, is rich in polyphenols and flavonoids and exhibits antibacterial, anti-inflammatory, and antioxidant effects [9].…”

Section: Introductionmentioning

confidence: 99%

Effects of Gnaphalium affine Extract on the Gel Properties of •OH-Induced Oxidation of Myofibrillar Proteins

Chang,

Hu,

Shi

et al. 2024

Foods

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This study aimed to investigate the effect of Gnaphalium affine extract (GAE) (0.04, 0.2 and 1 mg/g protein) on the gel properties of porcine myofibrillar proteins (MPs) in a simulated Fenton oxidation system, using tea polyphenols (TPs) at similar concentrations of 0.04, 0.2, and 1 mg/g protein, respectively, as a contrast. The findings revealed that as the TP concentration increased, the water retention of MP gels decreased significantly (p < 0.05). In contrast, MP gels containing medium and high concentrations of GAE exhibited significantly higher water retention than those with low concentrations of GAE (p < 0.05). When the concentration of GAE was increased to 1 mg/g protein, the strength of MP gels was significantly reduced (p < 0.05) by 33.32% compared with the oxidized control group, suggesting that low and medium GAE concentrations support MP gel formation. A texture profile analysis indicated that an appropriate GAE concentration improved gel structure and texture. Dynamic rheological characterization revealed that low concentrations of TP (0.04 mg/g protein) and low and medium concentrations of GAE (0.04 and 0.2 mg/g protein) strengthened the protein gel system. Conversely, high concentrations of TP and GAE (1.0 mg/g protein) damaged the protein gel system or even promoted the collapse of the gel system. Scanning electron microscopy revealed that higher TP concentrations disrupted the gel, whereas low and medium GAE concentrations maintained a more continuous and complete gel network structure compared with the oxidized control group. This indicates that an appropriate GAE concentration could effectively hinder the destruction of the gel network structure by oxidation. Therefore, based on the obtained results, 0.2 mg/g protein is recommended as the ideal concentration of GAE to be used in actual meat processing to regulate the oxidization and gel properties of meat products.

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Section: Introductionmentioning

confidence: 99%

Effects of Gnaphalium affine Extract on the Gel Properties of •OH-Induced Oxidation of Myofibrillar Proteins

Chang,

Hu,

Shi

et al. 2024

Foods

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“…The texture of processed meat products, especially comminuted meat products, is highly dependent on the gel network structure as well as the matrix components, fat droplets, and water molecules in three-dimensional networks. Myofibrillar protein (MP) is the main component of meat, accounting for about 60% of the total protein. , Upon heat treatment, MP can form a gel structure and provide adhesive force to stabilize water molecules and fat droplets in the gel network structure, thus playing an important role in stabilizing the texture and water retention of meat products. , However, MP is susceptible to various stresses during transportation, storage, and processing, which can lead to changes in its physical, chemical, and structural properties, thereby reducing its cementitious properties and the quality of the final product. Usually, during meat processing, food additives are often added to meat products to improve the water holding capacity (WHC) of meat products and improve the appearance and quality of products .…”

Section: Introductionmentioning

confidence: 99%

“…The results revealed that “clean label” skin functional protein powders prepared by the drying wetting method possess superior properties and exhibit great potential to be applied in the food industry. Besides, it has been reported that the thermal-induced gelation of MP molecules involves denaturation, irreversible aggregation, and formation of three-dimensional networks, and the gel properties can be highly influenced by proteins, polysaccharides, and other additives. ,, In the case of the prepared “clean label” skin functional protein powders, side chain groups of collagen protein can theoretically interact with the MP molecules through multiple interactions such as hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bonds. However, the influence of “clean label” protein powder additives on MP gel and its mechanism have yet to be fully investigated.…”

Section: Introductionmentioning

confidence: 99%

“…Myofibrillar protein (MP) is the main component of meat, accounting for about 60% of the total protein. 1,2 Upon heat treatment, MP can form a gel structure and provide adhesive force to stabilize water molecules and fat droplets in the gel network structure, thus playing an important role in stabilizing the texture and water retention of meat products. 3,4 However, MP is susceptible to various stresses during transportation, storage, and processing, which can lead to changes in its physical, chemical, and structural properties, 5 thereby reducing its cementitious properties and the quality of the final product.…”

Section: ■ Introductionmentioning

confidence: 99%

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Mechanism on the Synergistic Gelation of the Myofibrillar Protein Composite Gel Enhanced by “Clean-Label” Skin Functional Protein Powders

Chen,

Zhang,

Dai

et al. 2023

J. Agric. Food Chem.

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The concept of healthiness and sustainability has promoted the innovation and development of "clean-label" products. Herein, this study aims to explore the influence mechanism of "clean label" skin protein powder (FPP) on the gelation properties of myofibrillar proteins (MPs). Specifically, the addition of FPP (0.2−4.0%) can improve the water holding capability and texture properties of MP composite gels. When the FPP concentration is over 1.0%, the composite gels exhibit no significant water loss during centrifugation. Dynamic rheology and sodium-dodecyl sulfate-polyacrylamide gel electrophoresis results revealed that FPP can slow the aggregation and denaturation of myosin and promote the formation of disulfide bonds between myofibril proteins, thus forming a stable network structure. Structural observation revealed that FPP can fill into the MP gel and lead to the formation of compact gel structures. Besides, with the increase of FPP concentration, the chemical forces involved in structural stabilization change significantly. Specifically, hydrophobic interaction and hydrogen bonding are the dominant forces at a lower FPP concentration (0.2 and 0.4%), while the ionic bond and disulfide bond are the dominant forces at a higher concentration. Overall, this work demonstrated that FPP can significantly improve the gel functionality of MP by altering the gel structure and strengthening the molecular forces.

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Effect of γ‐oryzanol/β‐sitosterol‐based oleogels on the physicochemical and gel properties of Nemipterus virgatus myofibrillar protein

Mi,

Yang,

et al. 2024

J Sci Food Agric

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BACKGROUNDThe effect of oleogels prepared with peanut oil and different concentrations of γ‐oryzanol and β‐sitosterol mixture (γ/β; 20, 40, 60, 80 and 100 g kg−1) on the physicochemical and gel properties of myofibrillar protein (MP) was investigated.RESULTSThe solubility and average particle size of MP first decreased and then increased with increasing γ/β concentration. Peanut oil or oleogels could induce the exposure of hydrophobic amino acids and the unfolding of MP, thus significantly increasing the surface hydrophobicity, sulfhydryl content and absolute value of zeta potential, which reached maximum values when the γ/β concentration was 60 g kg−1 (P < 0.05). The addition of peanut oil decreased the gel strength and water holding capacity of MP gel. However, oleogels prepared with 60 g kg−1 γ/β could significantly increase the hydrophobic interactions and disulfide bond content of MP gel (P < 0.05), which promoted the crosslinking and aggregation of MP, enhancing the gel properties. Peanut oil had no significant influence on the secondary structure of MP, while oleogels promoted the transition of MP conformation from α‐helix to β‐sheet structure. The results of light microscopy and confocal laser scanning microscopy indicated that oleogels prepared with 60 g kg−1 γ/β filled in the pores of MP gel network to form denser and more uniform structure.CONCLUSIONOleogels prepared with 60 g kg−1 γ/β could effectively improve the quality of MP gel and have promising application prospects in surimi products. © 2024 Society of Chemical Industry.

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Concentration-dependent effect of eugenol on porcine myofibrillar protein gel formation

Cited by 12 publications

References 52 publications

Effects of Gnaphalium affine Extract on the Gel Properties of •OH-Induced Oxidation of Myofibrillar Proteins

Effects of Gnaphalium affine Extract on the Gel Properties of •OH-Induced Oxidation of Myofibrillar Proteins

Mechanism on the Synergistic Gelation of the Myofibrillar Protein Composite Gel Enhanced by “Clean-Label” Skin Functional Protein Powders

Effect of γ‐oryzanol/β‐sitosterol‐based oleogels on the physicochemical and gel properties of Nemipterus virgatus myofibrillar protein

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