Glutamate dehydrogenase was purifiedfrom thecrudeextract of Pseudomonas pseudoal caligenes.Theenzyme had a molecular weight of 290 000 and was composed of six subunits with identical molecular weightof47 000 . The enz...Glutamate dehydrogenase was purifiedfrom thecrudeextract of Pseudomonas pseudoal caligenes.Theenzyme had a molecular weight of 290 000 and was composed of six subunits with identical molecular weightof47 000 . The enzyme was highly specific for NADP(H) and the sub strates.The biochemicalpropertiessuch askineticparametersand heatstability werealsoexamined. The purified GDHshowed considerableloss ofactivity uponfreezing.展开更多
产β-甘露聚糖酶的罗耳阿太菌（Athelia roffsii）菌株CBS191．62，发酵培养5日，发酵液离心去菌体，上清经硫酸铵沉淀，琼脂糖凝胶（DEAE Sepharose Fast Flow）层析、羟基磷灰石（Hydroxylapatite）层析和冷冻干燥等步骤，β-甘露聚...产β-甘露聚糖酶的罗耳阿太菌（Athelia roffsii）菌株CBS191．62，发酵培养5日，发酵液离心去菌体，上清经硫酸铵沉淀，琼脂糖凝胶（DEAE Sepharose Fast Flow）层析、羟基磷灰石（Hydroxylapatite）层析和冷冻干燥等步骤，β-甘露聚糖酶的比活提高了15．1倍，获得凝胶电泳均一的蛋白样品。经SDS-PAGE测定β-甘露聚糖酶分子量为42kDa，证明该酶为单聚体；用等电聚焦电泳测得其等电点为2．95；该酶的最适反应温度为30℃，在不超过50℃时酶活较稳定；酶反应的最适pH为5．0，pH稳定范围为5．5～7．0。重金属离子Zn^2＋、Fe^3＋、Co^2＋、Hg^2＋能强烈抑制该酶活性，而Mg^2＋、Al^3＋对该酶有部分的抑制作用，低浓度的Li＋、Mn^2＋、Ca^2＋对该酶基本没有影响。展开更多
文摘Glutamate dehydrogenase was purifiedfrom thecrudeextract of Pseudomonas pseudoal caligenes.Theenzyme had a molecular weight of 290 000 and was composed of six subunits with identical molecular weightof47 000 . The enzyme was highly specific for NADP(H) and the sub strates.The biochemicalpropertiessuch askineticparametersand heatstability werealsoexamined. The purified GDHshowed considerableloss ofactivity uponfreezing.
文摘产β-甘露聚糖酶的罗耳阿太菌（Athelia roffsii）菌株CBS191．62，发酵培养5日，发酵液离心去菌体，上清经硫酸铵沉淀，琼脂糖凝胶（DEAE Sepharose Fast Flow）层析、羟基磷灰石（Hydroxylapatite）层析和冷冻干燥等步骤，β-甘露聚糖酶的比活提高了15．1倍，获得凝胶电泳均一的蛋白样品。经SDS-PAGE测定β-甘露聚糖酶分子量为42kDa，证明该酶为单聚体；用等电聚焦电泳测得其等电点为2．95；该酶的最适反应温度为30℃，在不超过50℃时酶活较稳定；酶反应的最适pH为5．0，pH稳定范围为5．5～7．0。重金属离子Zn^2＋、Fe^3＋、Co^2＋、Hg^2＋能强烈抑制该酶活性，而Mg^2＋、Al^3＋对该酶有部分的抑制作用，低浓度的Li＋、Mn^2＋、Ca^2＋对该酶基本没有影响。
