Inhibition of Epigallocatechin-3-gallate/Protein Interaction by Methyl-β-cyclodextrin in Myofibrillar Protein Emulsion Gels under Oxidative Stress

Zhang, Yumeng; Lv, Yuanqi; Chen, Lin; Wu, Haizhou; Zhang, Yingyang; Suo, Zhiyao; Wang, Shuxin; Liang, Yuxin; Xu, Xinglian; Zhou, Guanghong; Feng, Xianchao

doi:10.1021/acs.jafc.8b00275

Cited by 30 publications

(16 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Compared to MS A, a decrease in the fluorescence intensity of MS B was observed, indicating the exposure of interior tryptophan and tyrosine residues of myosin to a polar microenvironment (Figure ). This may be attributed to the fact that ·OH may have induced myosin to unfold, exposing the interior tryptophan and tyrosine residues at the surface . In addition, it is well known that tryptophan and tyrosine are easy to oxidize; therefore, the exposed tryptophan and tyrosine residues may have been oxidized, leading to a decrease in the fluorescence intensity.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

l-Arginine and l-Lysine Alleviate Myosin from Oxidation: Their Role in Maintaining Myosin’s Emulsifying Properties

Zhang

Huang

et al. 2021

J. Agric. Food Chem.

View full text Add to dashboard Cite

This study investigated the alleviative effects of l-arginine and l-lysine on the emulsifying properties and structural changes of myosin under hydroxyl radical (·OH) stress. The results showed that ·OH decreased the emulsifying activity index and emulsifying stability index but increased the creaming index and droplet size of a soybean oil–myosin emulsion (SOME). Confocal laser scanning microscopy demonstrated that ·OH caused larger and more inhomogeneous SOME droplets. l-Arginine and l-lysine effectively alleviated ·OH-induced destructive effects on the emulsifying properties of myosin. In addition, ·OH increased the extent of protein carbonylation and dityrosine formation, surface hydrophobicity, and β-sheet content, but decreased the tryptophan fluorescence intensity, solubility, total sulfhydryl, and α-helix content of myosin. Although l-lysine increased dityrosine fluorescence intensity, l-arginine and l-lysine effectively alleviated the aforementioned structural changes of myosin. Therefore, l-arginine and l-lysine could mitigate ·OH-induced structural changes of myosin, which enabled myosin to maintain its emulsifying capacity under oxidative stress.

show abstract

Section: Resultsmentioning

confidence: 99%

“…Surface hydrophobicity represents the distribution of hydrophobic residues on the surface of a protein and is an important indicator of the protein unfolding process . As illustrated in Figure , MS B had significantly higher surface hydrophobicity than MS A ( P < 0.05), indicating that ·OH induced the unfolding of myosin.…”

Section: Resultsmentioning

confidence: 99%

l-Arginine and l-Lysine Alleviate Myosin from Oxidation: Their Role in Maintaining Myosin’s Emulsifying Properties

Zhang

Huang

et al. 2021

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…Zhang, Lv, et al. (2018) found that methyl‐β‐cyclodextrin (M‐β‐CD) was effective in increasing the polyphenol loading capacity by interfering with protein–phenol interactions. The increased cooking loss of the MP f emulsion gel caused by high concentrations of EGCG was offset by the addition of M‐β‐CD in a dose‐dependent manner.…”

Section: Effect Of Phytophenol Binding On Structure‐related Muscle Protein Functionalitymentioning

confidence: 99%

Myoprotein–phytophenol interaction: Implications for muscle food structure‐forming properties

Guo

Xiong

2021

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

Phenolic compounds are commonly incorporated into muscle foods to inhibit lipid oxidation and modify product flavor. Those that are present in or extracted from plant sources (seeds, leaves, and stems) known as “phytophenols” are of particular importance in the current meat industry due to natural origins, diversity, and safety record. Apart from these primary roles as antioxidants and flavorings, phytophenols are now recognized to be chemically reactive with a variety of food constituents, including proteins. In processed muscle foods, where the structure‐forming ability is critical to a product's texture‐related quality attributes and palatability, the functional properties of proteins, especially gelation and emulsification, play an essential role. A vast amount of recent studies has been devoted to protein–phenol interactions to investigate the impact on meat product texture and flavor. Considerable efforts have been made to elucidate the specific roles of phytophenol interaction with “myoproteins” (i.e., muscle‐derived proteins) probing the structure‐forming process in cooked meat products. The present review provides an insight into the actions of phytophenols in modifying and interacting with muscle proteins with an emphasis on the reaction mechanisms, detection methods, protein functionality, and implications for structural characteristics and textural properties of muscle foods.

show abstract

“…Meanwhile, the high rotational speed also produces intense laminar, turbulent, and cavitation effects, to mix the food quickly and uniformly. Due to these characteristics of HSH, it is widely used for protein emulsifier preparation . However, the HSH speeds used in these studies are not fixed, and it is worthwhile studying the conditions under which MPs can be properly denatured to enhance their emulsification properties.…”

Section: Introductionmentioning

confidence: 99%

“…Due to these characteristics of HSH, it is widely used for protein emulsifier preparation. [12][13][14] However, the HSH speeds used in these studies are not fixed, and it is worthwhile studying the conditions under which MPs can be properly denatured to enhance their emulsification properties.…”

Section: Introductionmentioning

confidence: 99%

Effects of high‐speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low‐fat conditions

et al. 2019

View full text Add to dashboard Cite

BACKGROUND Emulsification is important for food quality and processing functionality. Most emulsification occurs under high‐fat conditions that eventually cause health concerns. Protein emulsifiers also have drawbacks such as lower dispersity. This study considered the effects of different high‐speed shear homogenization (HSH) speeds on the emulsifying and structural properties of myofibrillar proteins (MPs) under low‐fat conditions. RESULTS High‐speed shear homogenization significantly increased the emulsifying activity and emulsifying stability of MPs at lower speeds (8000 to 14 500 rpm). The primary structure of MP was not altered significantly by HSH, whereas its secondary, tertiary, and quaternary structures were changed. Particle size decreased first and then increased significantly, and reached a minimum when the HSH speed was 14 500 rpm. The absolute zeta potential values increased significantly and the dendritic fibrous structure of sample was destroyed when the speed exceeded 14 500 rpm. High‐speed shear homogenization (14 500 rpm) decreased the particle size and unfolded the protein, which improved the emulsifying properties of MPs. Excessive HSH speeds (20 500 rpm or higher) caused an aggregation of MP molecules, which was not conducive to improving their emulsifying properties. CONCLUSION Optimal HSH speed was achieved at 14 500 rpm to modify MPs' emulsifying and structural properties under low‐fatconditions. © 2019 Society of Chemical Industry

show abstract

Inhibition of Epigallocatechin-3-gallate/Protein Interaction by Methyl-β-cyclodextrin in Myofibrillar Protein Emulsion Gels under Oxidative Stress

Cited by 30 publications

References 39 publications

l-Arginine and l-Lysine Alleviate Myosin from Oxidation: Their Role in Maintaining Myosin’s Emulsifying Properties

l-Arginine and l-Lysine Alleviate Myosin from Oxidation: Their Role in Maintaining Myosin’s Emulsifying Properties

Myoprotein–phytophenol interaction: Implications for muscle food structure‐forming properties

Effects of high‐speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low‐fat conditions

Contact Info

Product

Resources

About