首页 | 本学科首页   官方微博 | 高级检索  
     

酸性α-淀粉酶的分离纯化与酶学性质研究
引用本文:胡元森,潘涛,李翠香. 酸性α-淀粉酶的分离纯化与酶学性质研究[J]. 生物技术通报, 2010, 0(3)
作者姓名:胡元森  潘涛  李翠香
作者单位:河南工业大学生物工程学院,河南工业大学粮油重点实验室与工程中心,郑州,450052
基金项目:河南工业大学博士基金项目 
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。

关 键 词:酸性α-淀粉酶  蛋白纯化  酶学性质  Acid-stable α-amylase

Purification and Properties of an Acid-stable Alpha-amylase from Bacillus subtilis
Hu Yuansen,Pan Tao,Li Cuixiang. Purification and Properties of an Acid-stable Alpha-amylase from Bacillus subtilis[J]. Biotechnology Bulletin, 2010, 0(3)
Authors:Hu Yuansen  Pan Tao  Li Cuixiang
Affiliation:Hu Yuansen Pan Tao Li Cuixiang(Bioengineering College,Henan University of Technology,Key Lab , Engineering Centre of Food , Oil in Henan University of Technology,Zhengzhou 450052)
Abstract: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.
Keywords:Protein purification  Enzymatic properties
本文献已被 CNKI 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号