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Novel thermostable lipase from Bacillus circulans IIIB153: comparison with the mesostable homologue at sequence and structure level

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Title Novel thermostable lipase from Bacillus circulans IIIB153: comparison with the mesostable homologue at sequence and structure level
 
Creator Johri, S.
Bhat, A.
Sayed, S.
Nargotra, A.
Jain, A.
Qazi, G. N.
 
Subject Biological Sciences
 
Description Thermophilic Bacillus circulans IIIB153 isolated from hot springs of North West Himalayas, India, produced an extracellular lipase, which exhibited significant
biofilm disruption property on the static biofilm disruption
model with a single species of Actinomyces viscosous. The
gene encoding the lipase was cloned and overexpressed in
Escherichia coli. Recombinant Bacillus circulans lipase
(BCL), a monomer with molecular mass of 43 kDa also
exhibited significant biofilm disruption activity. The enzyme was optimally active at 60�C, pH 8.5 and retained[70% of its original activity after 1 h incubation at 60�C. 3D structure of BCL developed by homology modeling showed a typical a/b hydrolase fold, a characteristic feature of lipolytic enzymes. Comparison of thermostable BCL with mesostable lipase from Chromobacterium viscosum at the sequence and structure level showed distinct variations in the structural features, with the presence of a high content of proline residues, aromatic amino acids and salt bridges. These features along with the presence of zinc-binding site observed in BCL structure could have a potential role in thermal stability of the enzyme.
 
Date 2011
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://iiim.csircentral.net/304/1/10.1007s11274-011-0808-1.pdf
Johri, S. and Bhat, A. and Sayed, S. and Nargotra, A. and Jain, A. and Qazi, G. N. (2011) Novel thermostable lipase from Bacillus circulans IIIB153: comparison with the mesostable homologue at sequence and structure level. World Journal of Microbiology and Biotechnology. ISSN 0959-3993
 
Relation http://dx.doi.org/10.1007/s11274-011-0808-1
http://iiim.csircentral.net/304/