米曲霉氨基酰化酶的纯化及粗酶性质研究  

Study on Purification and Properties of Aminoacylase of Aspergilus oryzae

作　　者：张媛媛[1] 张彬[1] 

机构地区：[1]石家庄学院化工学院,河北石家庄050035

出　　处：《食品研究与开发》2016年第2期183-186,共4页Food Research and Development

摘　　要：利用硫酸铵分级盐析法从米曲霉L-09中提取氨基酰化酶,比活力为56.01 U/mg,纯化倍数为2.06,酶活力回收率为80%。详细研究该粗酶的酶学性质。结果表明,经盐析法提纯的粗酶最适pH为7,最适反应温度为55℃,在55℃下热稳定性良好。溶液中的金属离子对酶活力有很大影响。其中,高浓度的Fe^(2+)、Mn^(2+)和Ca^(2+)对酶活力有抑制作用,低浓度的Co^(2+)离子对酶活力有激活作用。The aminoacylase from Aspergillus oryzae was partially purified by ammonium sulfate fractionation.The specific activity of aminoacylase was 56.01 U/mg.The purification ratio and recovery were 2.06 and 80%.The optimal pH of aminoacylase was 7.0.The optimal temperature of aminoacylase was 55 ℃.The thermal stability of aminoacylase under 55 ℃ was good.The ions in the solvent infected the aminoacylase.Fe^2＋,Mn^2＋and Ca^2＋ in high concentration lowered the activity of aminoacylase,the Co^2＋ in low concentration activated the aminoacylase.

关 键 词：氨基酰化酶 纯化 粗酶性质 

分 类 号：O629.8[理学—有机化学]