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Insoluble but enzymatically active α-amylase from Bacillus licheniformis

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Abstract

The gene encoding thermostable α-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 α-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.

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Abbreviations

CAZy:

Carbohydrate-Active enZyme

CBB:

Coomassie brilliant blue

GHs:

glycoside hydrolases

IPTG:

isopropyl-β-D-thiogalactopyranoside

LB:

Luria Bertani

PAGE:

polyacrylamide gel electrophoresis

PCR:

polymerase chain reaction

SDS:

sodium dodecyl sulfate

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Authors and Affiliations

  1. School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan

    Naeem Rashid, Alia Farooq & Muhammad Akhtar

  2. Institute of Industrial Biotechnology, Government College University, Lahore, 54000, Pakistan

    Alia Farooq &  Ikram-ul-Haq

Authors
  1. Naeem Rashid
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  2. Alia Farooq
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  3. Ikram-ul-Haq
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  4. Muhammad Akhtar
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Correspondence to Naeem Rashid.

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Rashid, N., Farooq, A., Ikram-ul-Haq et al. Insoluble but enzymatically active α-amylase from Bacillus licheniformis . Biologia 64, 660–663 (2009). https://doi.org/10.2478/s11756-009-0132-5

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  • DOI: https://doi.org/10.2478/s11756-009-0132-5

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