Insoluble but enzymatically active α-amylase from Bacillus licheniformis View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2009-08

AUTHORS

Naeem Rashid, Alia Farooq, Ikram-ul-Haq, Muhammad Akhtar

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. More... »

PAGES

660-663

Journal

TITLE

Biologia

ISSUE

4

VOLUME

64

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.2478/s11756-009-0132-5

DOI

http://dx.doi.org/10.2478/s11756-009-0132-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019857153


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