Abstract: 【Objective】 To determine the physiochemical properties and biological functions of the laccase from the fruiting bodies of wild Agaricus balchaschensis, this study to explore the biological characteristics of the fruiting bodies, the physiochemical properties of the laccase, and the degradation ability of phenolic compoundstheoretical basis for the cultivation domestication of wild A. balchaschensis, as well as the efficient use of cultivating materials. 【Methods】 Cellulose CM-cellulose cation exchange column, Q-Sepharose anion exchange column, and Superdex 75 gel chromatography filtration and purification technique were used to analyze the degradative metabolic substrate of the laccase and its inhibition ability against metal ions. The optimum temperature and pH value for the activity laccase were determined. 【Results】 The laccase obtained from the fruiting bodies of A. balchaschensis was a 65 kDa single subunit protein. The total purification multiple was 354.58 and the specific activity was17.02 U/mg. The sequence of the 10 N-terminal amino acids of the enzyme was SGGPEQNTTA. Through NBCI-BLAST, it was found that the laccase was homologous to those of Pleurotus ostreatus and Versicolor Versicolor. The laccase was substrate-specific and varied greatly based on different metabolic substrates. The major metabolic substrates ranked from strong to weak were ABTS > dimethoxyphenol > toluidine. The optimum pH value was 2.2, so the laccase was acid-resistant. The optimum reaction temperature was 40℃, so the laccase was active at medium-low temperatures. Cu²⁺ can slightly promote the laccase to catalyze ABTS, while Hg²⁺ can strongly inhibit its catalysis of ABTS. 【Conclusion】 The results showed that the laccase from the fruiting bodies of A. balchaschensis was a 65 kDa single subunit protein.