Covalent grafting of one of the two flavonols (kaemperol and quercetin) to caseinate was achieved by a reaction between the heat-oxidized flavonols and caseinate at flavonol-lysine molar ratios of 1:100 and 1:200. Grafted caseinate products (GCPs) showed - NH2 content reduction and respective kaemperol and quercetin contents of 1.08-6.13 and 3.23-6.64 mmol/kg protein. Quercetin was more reactive than kaemperol under the same conditions, while long-time flavonol heat and higher flavonol-lysine molar ratio caused greater flavonol-grafting. GCPs subjected to 180-day storage had further flavonol-grafting, -NH2 content decrease, and weak protein crosslinking. GCPs consistently had higher surface hydrophobicity but lower emulsification and digestibility than caseinate, while greater flavonol-grafting caused a remarkable value change. Meanwhile, the Kjeldahl method was more suitable than the UV-absorption method to evaluate protein digestibility, because the grafted flavonols in this case did not interfere with data results. Collectively, the covalent flavonol-grafting of proteins can impact the assayed protein functionalities.
Keywords: Caseinate; Covalent grafting; Digestibility; Emulsifying property; Flavonol.
Copyright © 2022 Elsevier Ltd. All rights reserved.