摘要
新鲜苹果经匀浆、抽提、硫酸铵盐析、DEAE-Cellulose柱层析,获得纯化苹果过氧化氢酶(CAT)液。纯化CAT酶液蛋白含量26.8mg/mL,活力843Units/mL,比活力31.5Units/mg。经过温度和pH考察,酶的最适温度为50℃、最适pH值为5.0。金属离子影响为:Cu2+和Mn2+对该酶有不同程度的激活作用,Na+对该酶有一定程度的抑制作用。以过氧化氢为底物,Lineweaver-Burk双倒数作图法求得此酶的Km和Vmax分别为2.27mmol/L和2.5μmol/min。
A catalase from fresh apple was purified by saline extraction, ammonium sulfate precipition and DEAE-Cellulose column chromatography. The catalase extraction contained protein 26.8mg/mL, activity of 843Units/mL and specific activity of 31.5Units/mg. The catalase has an optimum activity of temperature at 50℃ and the optimum activity of pH value at 5.0 as regards affluences on activity of different temperature and pH values. The metal ions of Cu^2+ and Mn^2+ showed some degrees of activation, on the other hand, Na^+ showed some action of inhibition on the activity in various concentrations. The apparent Km and Vmax values were 2.27mmol/L and 2.51μmol/min respectively, which were determined by Lineweaver-Burk graphs method using hydrogen peroxide as the substance.
出处
《食品科技》
CAS
北大核心
2006年第11期66-68,共3页
Food Science and Technology
关键词
苹果
过氧化氢酶
纯化
性质
apple, catalase, purification, properties