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This study aimed to analyze the effect of hydrogen peroxide decolorization on the structure and functional characteristics of tea meal protein to provide some theoretical basis for the utilization of tea meal protein. The changes in the protein structure and function before and after decolorization were evaluated by measuring denaturation temperature, surface hydrophobicity, and sulfhydryl content and by analyzing infrared spectrum, X-ray diffraction peak, and microstructure, etc. Results showed that decolorization with hydrogen peroxide increased the surface hydrophobicity, decreased the sulfhydryl content, and did not change the disulfide bond content. The treatment weakened the chemical bond strength but did not affect the basic skeleton structure. The microstructure as well as the position and intensity of the X-ray diffraction peak of the protein from Camellia oleracea seed cake remained the same before and after the treatment. The heat denaturation temperature also increased. Hydrogen peroxide did not change the isoelectric point; decreased the solubility, emulsifying properties, emulsion stability, foaming ability, and foam stability of the protein; and increased the oil and water holding capacities. Overall, decolorization with hydrogen peroxide did not significantly affect the protein structure but changed its functional properties.
Yao et al. (Tue,) studied this question.