Insoluble but enzymatically active a-amylase from Bacillus licheniformis

The gene encoding thermostable a-amylase from Bacillus licheniformis consisting of 483 amino acid residues (mature protein) was cloned and expressed in Escherichia coli under the control of T7 promoter. The analysis of the soluble and insoluble fractions after lyzing the host cells revealed that rec...

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Bibliographic Details
Published in:Biológia 2009-08, Vol.64 (4), p.660-663
Main Authors: Rashid, Naeem, Farooq, Alia, Ikram-Ul-Haq, Akhtar, Muhammad
Format: Article
Language:English
Subjects:
a-Amylase
Amino acids
Bacillus licheniformis
Enzymes
Escherichia coli
Promoters
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Summary:The gene encoding thermostable a-amylase from Bacillus licheniformis consisting of 483 amino acid residues (mature protein) was cloned and expressed in Escherichia coli under the control of T7 promoter. The analysis of the soluble and insoluble fractions after lyzing the host cells revealed that recombinant a-amylase was produced in insoluble aggregates. Despite being produced in the insoluble aggregates the recombinant enzyme was highly active with a specific activity of 408 U/mg.
ISSN:0006-3088
1336-9563
DOI:10.2478/s11756-009-0132-5