摘要
分离得到的假单胞菌(Pseudomonas sp) 菌株具有较强的分泌胞外弹性蛋白酶的能力。经微生物发酵方法生产的弹性蛋白酶,经过盐析、透析、DEAE SephadexA2 5离子交换层析、SephadexG75凝胶过滤层析等纯化步骤,从其发酵液中得到了均一的酶制品。研究结果表明,酶的最适作用温度为5 0℃;在硼砂-硼酸缓冲液中最适作用pH为8 0左右;酶在碱性环境下( pH7 0～12 0 )稳定性较好;在37℃以下,酶的稳定性较高。超过6 0℃。
An extracellular Elastase secreted by a Pseudomonas sp strain was isolated in the laboratory A crude enzyme solution from the culture fluid of Pseudomonas sp was purified to SDS-PAGE homogeneity by (NH_4)_2SO_4 precipitation, Anion-exchange chromatography of DEAE-Sephadex A25 and Gel-filtration chromatography on Sephadex G75 The elastase showed two peaks by HPLC and its molecular weight was estimated to be 32 ku by SDS-PAGE The optimum condition for elastolytic activity was pH7 8, temperature 50℃ The enzyme was stable in the alkaline condition (pH7 0～12) This enzyme is stable below 37℃ while it lost nearly all its activity within short time above 60℃
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2005年第4期10-13,共4页
Food and Fermentation Industries
基金
国家 8 63计划 (No .2 0 0 2AA2 4 80 31 )资助项目
