article · Journal of Food Science
Whey protein isolate can be covalently bound to rosmarinic acid using either alkaline conditions at pH 9 or enzymatic treatment with tyrosinase in the presence of air at room temperature. Both methods induce structural changes in the protein, evidenced by shifts in intrinsic fluorescence and hydrophobic dye binding, alongside reductions in free amino groups, thiol groups, and tryptophan content. The alkaline approach results in greater structural modification and yields conjugates with higher antioxidative capacity. Conversely, the enzymatic route results in lesser reductions of functional groups but produces conjugates displaying mild antimicrobial activity against two strains of Staphylococcus aureus. Covalently coupling rosmarinic acid with whey protein modifies the protein structure and functional traits, offering potential utility as a multifunctional food ingredient combining protein functionality with the health benefits of phenolic compounds.
Proteins in food products frequently require enhanced functionality, including protective traits against oxidation and microbial contamination. By chemically or enzymatically linking a natural antioxidant compound to dairy proteins, food developers can create dual-purpose ingredients. This approach improves antioxidant performance and targeted antimicrobial activity, potentially helping to extend product quality and deliver additional dietary health benefits.
The abstract suggests these conjugates could serve as multifunctional ingredients in diverse food products, integrating the health-promoting benefits of phenolic compounds. Target users would be food manufacturers formulating functional or fortified foods. The research is early-stage laboratory work, having demonstrated chemical modification, antioxidant potential, and mild antibacterial efficacy in vitro without testing inside actual food matrices or pilot manufacturing environments.
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The covalent interactions between whey protein isolate (WPI) and rosmarinic acid (RosA) at two different conditions, alkaline (pH 9) and enzymatic (in the presence of tyrosinase, PPO), at room temperature with free atmospheric air were studied. The conjugates formed between WPI and RosA were characterized in terms of their physicochemical and functional properties. The changes in protein structure were analyzed by intrinsic fluorescence and binding of 8-anilino-1-naphthalenesulfonic acid. The findings show that the covalent interactions caused a decrease in free amino and thiol groups and tryptophan content at both conditions. The decrease at enzymatic conditions was lower than at alkaline conditions. In addition, modified WPI at alkaline conditions exhibited higher antioxidative capacity compared to the modification at enzymatic conditions. However, WPI modified at enzymatic condition showed mild antimicrobial activity against Staphylococcus aureus LMG 10147 and MU50 compared to WPI modified at alkaline conditions and unmodified WPI (control). The modified WPI can be used as multifunctional ingredient into various food products with an additional health promoting effect of the bound phenolic compounds.
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DOI: 10.1111/1750-3841.14222
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