Comparison of interaction, structure, and cell proliferation of α‐lactalbumin–safflower yellow complex induced by microwave heating or conventional heating

Abstract Background The protein–polyphenol interaction mechanism has always been a research hotspot, but their interaction is affected by heat treatment, which is widely applied in food processing. Moreover, the effects of microwave or water‐bath heating on the protein–polyphenol interaction mechanism have been not clarified. The pasteurization condition (65 °C, 30 min) was selected to compare the effects of microwave or water bath on binding behavior, structure, and cell proliferation between α ‐lactalbumin ( α ‐LA) and safflower yellow (SY), thus providing a guide for the selection of functional dairy processing conditions. Results Microwave heat treatment of α ‐LA–SY resulted in stronger fluorescence quenching than that of conventional heat treatment. Moreover, the binding constant K a of all α ‐LA–SY samples was augmented significantly after microwave or water bath treatment, and microwave‐heated α ‐LA–SY showed the maximum K a . Fourier transform infrared spectroscopy showed that microwave heating resulted in more ordered structures of α ‐LA into its disordered structures than water bath heating. However, the ferric reducing antioxidant power and chroma value of α ‐LA–SY were more reduced by microwave heating than by water bath heating. Moreover, microwave heating facilitated the cell proliferation of α ‐LA–SY compared with water bath treatment. Conclusion It was demonstrated that microwave heating promoted interaction between α ‐LA and SY more than water bath heating did. Microwave heat treatment was a safe and effective way to enhance the binding affinity of α ‐LA to SY, being a potential application in food industry. © 2022 Society of Chemical Industry.