Changes in Structural and Gel Properties of Myofibrillar Proteins Induced by Sodium Chloride and Hydroxyl Radical

Han, Yurui; Shen, Hui; Zhao, Ming; Sun, Weizheng

doi:10.3136/fstr.25.97

Cited by 5 publications

(6 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gel strength is a good indicator of the structural integrity of proteins and their ability to form a gel mesh. The process of forming a gel mesh by thermal induction of DMPs involves denaturation of proteins by increased temperature, mutual agglutination between proteins, and mutual cross-linking, each of which affects the properties of the gel ( 12 ). As shown in Figure 3A , the gel strength decreased significantly ( p < 0.05) with increasing concentrations of H 2 O 2 .…”

Section: Resultsmentioning

confidence: 99%

“…Rheological properties were measured for protein-protein interactions and the formation of gel mesh during the formation of gels from protein solutions ( 12 ). The storage modulus (G′) and loss modulus (G″) of the DMPs solution are important parameters of the rheological properties.…”

Section: Resultsmentioning

confidence: 99%

“…Rheological properties were measured for protein-protein interactions and the formation of gel mesh during the formation of gels from protein solutions (12) ′′ continued to increase slowly because of the stretching of most myosin structures and coalescence, leading to the formation of an orderly gel mesh structure (44). As shown in Figure 5B, the final G ′′ of the warming process significantly decreased by 65.7% when the hydroxyl radical concentration was 12 mmol/L compared to the value in the blank group (p < 0.05).…”

Section: Rheological Property Analysismentioning

confidence: 99%

“…However, the gelation properties of duck breast muscle remain unclear. Gelling properties depend on several intrinsic factors, including the meat species, muscle type, and fiber type ( 12 ). Researchers have used a hydroxyl radical system to simulate systematic muscle oxidation in vitro to better understand the mechanism underlying the effect of protein oxidation on meat gelation.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Physicochemical properties and gel-forming ability changes of duck myofibrillar protein induced by hydroxyl radical oxidizing systems

Zhu

Shi²,

Liu³

et al. 2022

Front. Nutr.

View full text Add to dashboard Cite

This paper focuses on the changes of physicochemical properties and gel-forming ability of duck myofibrillar proteins (DMPs) induced using hydroxyl radical oxidizing systems. DMPs were firstly extracted and then oxidized at various H2O2 concentrations (0, 4, 8, and 12 mmol/L) using Fenton reagent (Fe3+-Vc-H2O2) to generate hydroxyl radicals, and the effects of hydroxyl radical oxidation on the physicochemical changes and heat-induced gel-forming capacity of DMPs were analyzed. We observed obvious increases in the carbonyl content (p < 0.05) and surface hydrophobicity of DMPs with increasing of H2O2 concentrations (0–12 mmol/L). In contrast, the free thiol content (p < 0.05) and water retention ability of DMPs decreased with increasing H2O2 concentrations (0–12 mmol/L). These physicochemical changes suggested that high concentrations of hydroxyl radicals significantly altered the biochemical structure of DMPs, which was not conducive to the formation of a gel mesh structure. Furthermore, the gel properties were reduced based on the significant decrease in the water holding capacity (p < 0.05) and increased transformation of immobilized water of the heat-induced gel to free water (p < 0.05). With the increase of H2O2 concentrations, secondary structure of proteins analysis results indicated α-helix content decreased significantly (p < 0.05), however, random coil content increased (p < 0.05). And more cross-linked myosin heavy chains were detected at higher H2O2 concentrations groups through immunoblot analysis (p < 0.05). Therefore, as H2O2 concentrations increased, the gel mesh structure became loose and porous, and the storage modulus and loss modulus values also decreased during heating. These results demonstrated that excessive oxidation led to explicit cross-linking of DMPs, which negatively affected the gel-forming ability of DMPs. Hence, when processing duck meat products, the oxidation level of meat gel products should be controlled, or suitable antioxidants should be added.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Rheological Property Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Physicochemical properties and gel-forming ability changes of duck myofibrillar protein induced by hydroxyl radical oxidizing systems

Zhu

Shi²,

Liu³

et al. 2022

Front. Nutr.

View full text Add to dashboard Cite

show abstract

“…Ca 2+ can coordinate with proteins at the negative positions between adjacent protein molecules to form ionic bonds, and the electrostatic repulsion and hydrophobic interaction between proteins may be changed to induce the intermolecular polymerization, (Navarra et al., 2014 ; Zhou & Yang, 2019 ). Ionic strength was another important factor for meat processing and played a key role in the formation and enhancement of texture due to their ability to dissolve myofibrillar protein and also could improve the flavor of meat products and soup (Han et al., 2019 ).…”

Section: Resultsmentioning

confidence: 99%