Effective solubilization and single-step purification of Bacillus licheniformis α-amylase from insoluble aggregates

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• 作者：N. Rashid (1)
  N. Ahmed (1)
  M. Saleem Haider (1)
  I. Haque (2)
  
• 刊名：Folia Microbiologica
• 出版年：2010
• 出版时间：March 2010
• 年：2010
• 卷：55
• 期：2
• 页码：133-136
• 全文大小：510KB
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• 作者单位：N. Rashid (1)
  N. Ahmed (1)
  M. Saleem Haider (1)
  I. Haque (2)
  
  1. School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan
  2. Institute of Industrial Biotechnology, Government College University, Lahore, Pakistan
  

文摘

A high level expression of thermostable α-amylase gene from Bacillus licheniformis in Escherichia coli was obtained. The recombinant enzyme was mainly produced in the form of insoluble aggregates. The enzyme was solubilized without using denaturing agents and purified to homogeneity in a single step by ion exchange chromatography. The enzyme was purified 138-fold with a final yield of 349 %; the specific activity of the purified enzyme was 1343 U/mg.