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- Title
Functional characterization of hormone sensitive-like lipase from Bacillus halodurans: synthesis and recovery of pNP-laurate with high yields.
- Authors
Dua, Ashima; Gupta, Rani
- Abstract
The HSL-like lipase encoding gene ( Blip) from the polyextremophile Bacillus halodurans C-125 has been heterologously expressed in E.coli BL21(DE3). The enzyme is a monomer of ~42 kDa. It has extremely high thermal stability with a t of 35 min at 100 °C. Thermal denaturation/renaturation studies by CD and fluorescence analysis revealed complete refolding of the protein back to its native conformation even after 30 min at 90 °C. Blip prefers substrates with mid to long chain fatty acids. It has a higher catalytic efficiency on para-nitrophenyl fatty acyl esters as opposed to triacylglycerides ( k / K with pNP-palmitate as a substrate was 2.52 × 10 mM min while that with glyceryl tripalmitin was 4.06 × 10 mM min, respectively). The enzyme also has a unique selectivity for hydrolysis of unsaturated fatty acyl esters. The enzyme catalyses the synthesis of pNP-laurate with an optimized conversion of 95.94 ± 0.24%. A simple procedure for purification of the product has been developed that led to 89.91 ± 0.33% product recovery.
- Subjects
LIPASES; BACILLUS halodurans; ESTERIFICATION; ESCHERICHIA coli; THERMAL stability; ENZYMES; FATTY-acyl-CoA
- Publication
Extremophiles, 2017, Vol 21, Issue 5, p871
- ISSN
1431-0651
- Publication type
Article
- DOI
10.1007/s00792-017-0949-8