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

Fenhong Yang; Shuangshuang Jin; Xiaohan Li; Juan Shen; Xianming Zeng; Yaosong Wang; Guanghong Zhou; Changbo Tang

doi:10.1016/j.foodchem.2023.135818

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

Food Chem. 2023 Aug 1:416:135818. doi: 10.1016/j.foodchem.2023.135818. Epub 2023 Mar 5.

Authors

Fenhong Yang¹, Shuangshuang Jin¹, Xiaohan Li¹, Juan Shen¹, Xianming Zeng¹, Yaosong Wang², Guanghong Zhou³, Changbo Tang⁴

Affiliations

¹ Key Laboratory of Meat Processing, Ministry of Agriculture, Key Lab of Meat Processing and Quality Control, Ministry of Education, Jiangsu Collaborative Innovation Center of Meat Production and Processing, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China.
² College of Light Industry Science and Engineering, Nanjing Forestry University, Nanjing 210037, China.
³ Key Laboratory of Meat Processing, Ministry of Agriculture, Key Lab of Meat Processing and Quality Control, Ministry of Education, Jiangsu Collaborative Innovation Center of Meat Production and Processing, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: guanghong.zhou@hotmail.com.
⁴ Key Laboratory of Meat Processing, Ministry of Agriculture, Key Lab of Meat Processing and Quality Control, Ministry of Education, Jiangsu Collaborative Innovation Center of Meat Production and Processing, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: changbotang@hotmail.com.

PMID: 36893643
DOI: 10.1016/j.foodchem.2023.135818

Abstract

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 < 0.05). The α-helix structure of MP increased (p < 0.05) and MP gel properties enhanced slightly at low dosages of CA (10 and 50 μM), and both were impaired significantly (p < 0.05) at high dosages of CA (250 and 1250 μM). Two prominent adducts of myosin heavy chain (MHC)-BioC and Actin-BioC were identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), which gradually increased at low concentrations of BioC (10 and 50 μM), and raised significantly at the concentration of 1250 μM. According to the correlation analysis, MHC-BioC and Actin-BioC adducts showed a significant negative correlation with gel properties, such as G', hardness, and water holding capacity (WHC) (p < 0.01), which indicated that the covalent interactions between MP and CA significantly affected the quality of meat products.

Keywords: Biotinylated caffeic acid; Correlation analysis; Covalent interaction; Gel properties; Myofibrillar proteins.

MeSH terms

Actins* / metabolism
Caffeic Acids / analysis
Gels / chemistry
Myofibrils / chemistry
Phenol* / analysis
Phenols / analysis

Substances

Actins
caffeic acid
Phenol
Caffeic Acids
Phenols
Gels