Effective solubilization and single-step purification of Bacillus licheniformis alpha-amylase from insoluble aggregates.
A high level expression of thermostable alpha-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.
Rashid
N
N
School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan. naeemrashid37@hotmail.com
Ahmed
N
N
Saleem Haider
M
M
Haque
I
I
D001407:Bacillus / Q000737:chemistry / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D012995:Solubility; D000516:alpha-Amylases / Q000737:chemistry / Q000302:isolation & purification*
D001426:Bacterial Proteins; D000516:alpha-Amylases; C501919:alpha-amylase, Bacillus licheniformis