酸性α-淀粉酶的分离纯化与酶学性质研究  

Purification and Properties of an Acid-stable Alpha-amylase from Bacillus subtilis

作　　者：胡元森[1,2] 潘涛[1,2] 李翠香[1,2] 

机构地区：[1]河南工业大学生物工程学院 [2]河南工业大学粮油重点实验室与工程中心,郑州450052

出　　处：《生物技术通报》2010年第3期199-202,共4页Biotechnology Bulletin

基　　金：河南工业大学博士基金项目(150026)

摘　　要：纯化了枯草芽胞杆菌xm-1菌株酸性α-淀粉酶,并对其酶学性质进行了研究。通过硫酸铵沉淀和Sephadex G-75凝胶层析将酸性α-淀粉酶粗酶液纯化了32.5倍,活力回收率为10.0%。酶性质测定结果表明,该酸性α-淀粉酶分子量约为60kD,最适反应温度为45℃、最适作用pH5.0,该酶在pH3.4-6.0下稳定,高温耐受性差。Cu2+、Zn2+、EDTA对酶有不同程度的抑制作用,Ca2+和Mn2+对酶具有较强的激活作用。An acid-stable α-amylase produced by Bacillus subtilis xm-1 was purified and the properties was subsequently measured. The crude amylase was purified 32.5 times with 10.0% recovery of enzyme activity through ammonium sulfate precipitation and SephadexG-75 gel chromatography. The enzyme proerties showed that the molecular weight of the purified α-amylase was approximate 60 kD, and the optimum pH and temperature was 5.0 and 45℃ ,respectively. Metal ion of Cu^2＋ ,Zn^2＋ , EDTA inhibited α-amylase activity at various extent,while the Ca^2＋ and Mn^2＋ distinctly enhanced the activity.

关 键 词：酸性Α-淀粉酶 蛋白纯化 酶学性质 

分 类 号：Q814[生物学—生物工程]