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.
出处
《生物技术通报》
CAS
CSCD
北大核心
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)
关键词
酸性Α-淀粉酶
蛋白纯化
酶学性质
Acid-stable α-amylase Protein purification Enzymatic properties