[Objectives] This experiment was conducted to study the effects of malondialdehyde(MDA)on protein oxidation of soybean meal and the alleviation of tea polyphenols(TP). [Methods] Fresh soybean meal was divided into eight treatment groups, which was treated with 0,0.1,1 and 10 mmol·L-1 MDA, and also treated with 0,0.1,1 and 10 mmol·L-1 MDA and 0.6 mg·mL-1 TP, respectively, and the contents of carbonyl, sulfhydryl, and amino acid in soybean meal were determined. [Results]With the increasing concentration of MDA, the carbonyl content of soybean meal gradually increased(P<0.05),whereas the sulfhydryl and total sulfhydryl groups content, methionine, tyrosine, lysine contents, and in vitro digestibility of soybean meal protein decreased accordingly(P<0.05),the intrinsic fluorescence intensity of tryptophan increased first and then decreased, and its max peak was gradually blue-shifted, accompanied by an increase in the fluorescence intensity of Schiff base. In the oxidative group with the MDA concentration of 1 mmol·L-1, the carbonyl content in soybean meal significantly increased(P<0.05), the contents of sulfhydryl and total sulfhydryl groups significantly decreased(P<0.05),and the in vitro digestibility of soybean meal protein significantly decreased(P<0.01). In the high concentration MDA group (10 mmol·L-1),the carbonyl content in soybean meal significantly increased(P<0.01),and the contents of sulfhydryl and total sulfhydryl, the in vitro digestibility of soybean meal protein significantly decreased(P<0.01). Meanwhile, the methionine, tyrosine, lysine content in soybean meal were remarkably lower than those of the control group(P<0.05). TP addition could mitigate the increase of carbonyl content, the decrease of sulfhydryl and total sulfhydryl groups, the decrease of methionine content, the decrease of in vitro digestibility of soybean meal protein, the decrease of intrinsic fluorescence intensity of tryptophan and the increase of Schiff base content in soybean meal. [Conclusions]1 mmol·L-1MDA can trigger protein oxidation in soybean meal, resulting in a large change in the structure of soybean meal protein and the reduce in vitro digestibility of soybean meal protein. At this time,TP can effectively alleviate the MDA-induced protein oxidation in soybean meal and the reduced in vitro digestibility of soybean meal protein. [ABSTRACT FROM AUTHOR]