X-ray structure and characterization of a thermostable lipase from Geobacillus thermoleovorans

Thermo-alkalophilic bacterium, Geobacillus thermoleovorans secrets many enzymes including a 43 kDa extracellular lipase. Significant thermostability, organic solvent stability and wide substrate preferences for hydrolysis drew our attention to solve its structure by crystallography. The structure wa...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2019-01, Vol.508 (1), p.145-151
Main Authors: Moharana, Tushar Ranjan, Pal, Biswajit, Rao, Nalam Madhusudhana
Format: Article
Language:English
Subjects:
Activity
Crystal structure
Extremophile
Geobacillus thermoleovorans
Lipase
Thermostability
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Summary:Thermo-alkalophilic bacterium, Geobacillus thermoleovorans secrets many enzymes including a 43 kDa extracellular lipase. Significant thermostability, organic solvent stability and wide substrate preferences for hydrolysis drew our attention to solve its structure by crystallography. The structure was solved by molecular replacement method and refined up to 2.14 Å resolution. Structure of the lipase showed an alpha-beta fold with 19 α-helices and 10 β-sheets. The active site remains covered by a lid. One calcium and one zinc atom was found in the crystal. The structure showed a major difference (rmsd 5.6 Å) from its closest homolog in the amino acid region 191 to 203. Thermal unfolding of the lipase showed that the lipase is highly stable with Tm of 76 °C. 13C NMR spectra of products upon triglyceride hydrolysate revealed that the lipase hydrolyses at both sn-1 and sn-2 positions with equal efficiency.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2018.11.105