Effect of ultrasound treatment on interactions of whey protein isolate with rutin

Guo, Na; Ye, Shuang; Zhou, Ganghua; Zhang, Yimeng; Zhang, Fangyan; Xu, Jingjing; Pan, Shenyu; Zhu, Guilan; Wang, Ziying

doi:10.1016/j.ultsonch.2023.106387

Cited by 13 publications

(2 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Compared with the MFGM, the fluorescence intensity of the MFGM-SL complex decreased, and the fluorescence emission peak was redshifted at maximum wavelength, indicating that sonication changed the secondary structure of the protein, resulting in the expansion of the protein structure. Previous study has reported that sonication could affect whey protein-rutin interactions, which resulted in redshift at maximum wavelengths, which was consistent with our results [22] . In addition, the fluorescence intensity of the sonicated MFGM-SL complex (150 W–600 W) was lower than that of the unsonicated MFGM-SL complex, which could be due to low ultrasonic power treatment leading to quenching of fluorescence of exposed tryptophan residues [23] .…”

Section: Resultssupporting

confidence: 94%

Ultrasound modification on milk fat globule membrane and soy lecithin to improve the physicochemical properties, microstructure and stability of mimicking human milk fat emulsions

Ma,

Zhou,

Wang

et al. 2024

Ultrasonics Sonochemistry

View full text Add to dashboard Cite

Section: Resultssupporting

confidence: 94%

Ultrasound modification on milk fat globule membrane and soy lecithin to improve the physicochemical properties, microstructure and stability of mimicking human milk fat emulsions

Ma,

Zhou,

Wang

et al. 2024

Ultrasonics Sonochemistry

View full text Add to dashboard Cite

“…In addition, protein-polyphenol covalent complexes can also be used as nanomaterials. Because proteins are of amphipathic nature, complexes of protein-polyphenol have binding affinity for both hydrophilic and hydrophobic substances ( 128–130 ). Therefore, the use of phenolic-protein adducts as new carriers for unstable bioactive substances (namely phenolic compounds, fatty acids, hormones, other lipophilic and drugs) has recently become a hot topic ( 131 , 132 ).…”

Section: Polyphenol-protein Covalent Complexes In Food Applicationsmentioning

confidence: 99%

Covalent polyphenols-proteins interactions in food processing: formation mechanisms, quantification methods, bioactive effects, and applications

Zhang,

Huang,

Wang

et al. 2024

Front. Nutr.

View full text Add to dashboard Cite

Proteins and polyphenols are abundant in the daily diet of humans and their interactions influence, among other things, the texture, flavor, and bioaccessibility of food. There are two types of interactions between them: non-covalent interactions and covalent interactions, the latter being irreversible and more powerful. In this review, we systematically summarized advances in the investigation of possible mechanism underlying covalent polyphenols-proteins interaction in food processing, effect of different processing methods on covalent interaction, methods for characterizing covalent complexes, and impacts of covalent interactions on protein structure, function and nutritional value, as well as potential bioavailability of polyphenols. In terms of health promotion of the prepared covalent complexes, health effects such as antioxidant, hypoglycemic, regulation of intestinal microbiota and regulation of allergic reactions have been summarized. Also, the possible applications in food industry, especially as foaming agents, emulsifiers and nanomaterials have also been discussed. In order to offer directions for novel research on their interactions in food systems, nutritional value, and health properties in vivo, we considered the present challenges and future perspectives of the topic.

show abstract

Effects of sound energy on proteins and their complexes

Kozell,

Solomonov,

Shimanovich

2023

FEBS Letters

View full text Add to dashboard Cite

Mechanical energy in the form of ultrasound, and protein complexes intuitively have been considered as two distinct unrelated topics. However, in the past few years, increasingly more attention has been paid to the ability of ultrasound to induce chemical modifications on protein molecules that further change protein‐protein interaction and protein self‐assembling behavior. Despite efforts to decipher the exact structure and the behavior‐modifying effects of ultrasound on proteins, our current understanding of these aspects remains limited. The limitation arises from the complexity of both phenomena. Ultrasound produces multiple chemical, mechanical, and thermal effects in aqueous media. Proteins are dynamic molecules with diverse complexation mechanisms. This review provides an exhaustive analysis of the progress made in better understanding the role of ultrasound in protein complexation. It describes in detail how ultrasound affects an aqueous environment and the impact of each effect separately and when combined with the protein structure and fold, the protein‐protein interaction, and finally the protein self‐assembly. It specifically focuses on modifying role of ultrasound in amyloid self‐assembly, where the latter is associated with multiple neurodegenerative disorders.

show abstract

Effect of ultrasound treatment on interactions of whey protein isolate with rutin

Cited by 13 publications

References 36 publications

Ultrasound modification on milk fat globule membrane and soy lecithin to improve the physicochemical properties, microstructure and stability of mimicking human milk fat emulsions

Ultrasound modification on milk fat globule membrane and soy lecithin to improve the physicochemical properties, microstructure and stability of mimicking human milk fat emulsions

Covalent polyphenols-proteins interactions in food processing: formation mechanisms, quantification methods, bioactive effects, and applications

Effects of sound energy on proteins and their complexes

Contact Info

Product

Resources

About