Biotinylated caffeic acid covalent binding with myofibrillar proteins in alkaline conditions: Identification of protein-phenol adducts and alterations in protein properties

•Biotinylated caffeic acid (BioC) was synthesized for the identification of protein-phenol adducts.•MHC-BioC and Actin-BioC adducts were purified and quantified in myofibrillar proteins system.•Secondary structures of MP were changed by covalent binding with caffeic acid.•Caffeic acid binding showed...

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Veröffentlicht in:	Food chemistry 2023-08, Vol.416, p.135818-135818, Article 135818
Hauptverfasser:	Yang, Fenhong, Jin, Shuangshuang, Li, Xiaohan, Shen, Juan, Zeng, Xianming, Wang, Yaosong, Zhou, Guanghong, Tang, Changbo
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - metabolism Biotinylated caffeic acid Caffeic Acids - analysis Correlation analysis Covalent interaction Gel properties Gels - chemistry Myofibrillar proteins Myofibrils - chemistry Phenol - analysis Phenols - analysis
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Zusammenfassung:	•Biotinylated caffeic acid (BioC) was synthesized for the identification of protein-phenol adducts.•MHC-BioC and Actin-BioC adducts were purified and quantified in myofibrillar proteins system.•Secondary structures of MP were changed by covalent binding with caffeic acid.•Caffeic acid binding showed negative correlation with gel properties of myofibrillar proteins. In this study, the effects of covalent interactions between myofibrillar proteins (MP) and caffeic acid (CA) were investigated. Protein-phenol adducts were identified by biotinylated caffeic acid (BioC) used as a substitution of CA. The total sulfhydryls and free amines content were decreased (p
ISSN:	0308-8146 1873-7072
DOI:	10.1016/j.foodchem.2023.135818