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

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 & DEG;C, 30 min) was selected to compare the effects of microwave or water bath on binding behavior, structure, and cell proliferation between alpha-lactalbumin (alpha-LA) and safflower yellow (SY), thus providing a guide for the selection of functional dairy processing conditions. Results: Microwave heat treatment of alpha-LA-SY resulted in stronger fluorescence quenching than that of conventional heat treatment. Moreover, the binding constant K-a of all alpha-LA-SY samples was augmented significantly after microwave or water bath treatment, and microwave-heated alpha-LA-SY showed the maximum K-a. Fourier transform infrared spectroscopy showed that microwave heating resulted in more ordered structures of alpha-LA into its disordered structures than water bath heating. However, the ferric reducing antioxidant power and chroma value of alpha-LA-SY were more reduced by microwave heating than by water bath heating. Moreover, microwave heating facilitated the cell proliferation of alpha-LA-SY compared with water bath treatment. Conclusion: It was demonstrated that microwave heating promoted interaction between alpha-LA and SY more than water bath heating did. Microwave heat treatment was a safe and effective way to enhance the binding affinity of alpha-LA to SY, being a potential application in food industry. (C) 2022 Society of Chemical Industry.

Automated summary

Microwave heating promotes the interaction between alpha-lactalbumin and safflower yellow more effectively than water bath heating, enhancing the binding affinity of alpha-lactalbumin to safflower yellow.