Alcohol dehydrogenase is a key enzyme in the final synthesis of β-phenylethanol in Huangjiu yeast， which comes from the Ehrlich pathway. To explore the differences and enzymatic analysis of Adh1pHJ， the ADH1 of Saccharomyces cerevisiae HJ and Saccharomyces cerevisiae S288C were used as templates respectively to amplify the target gene by PCR. The expression plasmid pET-28a(+)-ADH1 were constructed， and transformed into Escherichia coli BL21(DE3) cells to obtain high expression induced by IPTG. The crude enzymes were obtained after ultrasonic fragmentation， and then purified by affinity chromatography with AKTA pure. Finally the enzymatic analysis were explored. Using phenylacetaldehyde as substrate， it was found that the enzyme activity(231.51 U/g) of Adh1pHJ was 13.79% higher than that of Adh1pS288C (203.48 U/g)， and the Km value of Adh1pHJ (0.524 μmol/L) was less than that of Adh1pS288C (0.759 μmol/L)， which indicated that the affinity between Adh1pHJ and substrate was higher. From the kcat/Km value， it is found that the catalytic efficiency of Adh1pHJ[0.406 L/(μmol·min)] is higher. The tolerance of Adh1pHJ to β-phenylethanol and ethanol was higher than that of Adh1pS288C. This study provides a method and theoretical basis for the analysis of the structure and properties of Adh1p， and also provides a reference for the industrial production and development of β- phenylethanol.