:Experiment on Baci llus , the β-glucosidase was purified to homogeneity by fractional ammo
nium sulphate precipi tation , ion-exchange chromatog raphy on DEAE-52 and Sephadex G-100 gilfilt
ration chromatog raphy , its properties and subst rate specif icities were studied .The results indicated
that the enzyme exhibited optimum activity at pH 7.0 and 50 ℃, and it' s a neutral enzyme
which kept good stability under the condi tion of hig h temperature .The activity of β-glucosidase w as
st rongly ef fected by metal io ns , enhanced by Fe2 +and inhibited by K+obviously

以芽孢杆菌作为试验材料,采用硫酸铵分级沉淀、DEAE-52离子交换层析、Sephadex G-100凝胶过滤方法分离纯化β-葡萄糖苷酶,并测定了其部分酶学性质。结果表明:该酶以水杨酸苷为底物时,最适pH值为7.0,最适温度为50℃,是一种中性酶,具有较好的热稳定性。金属离子对酶活性影响较大,其中Fe2+对酶的激活作用最为明显,而K+对酶有明显的抑制作用。 更多还原