Production, purification and characterization of thermostable lipase enzyme from a thermophilic bacillus sp

Abstract EN

A thermos table lipase produced by a newly isolated thermophiles Geobacillus sp.

strain was purified to apparent homogeneity to 2.7-fold using ammonium sulfate precipitation followed by Q-Sepharose column chromatography.

The purified enzyme is a monomeric protein having molecular weight of 33 kDa.

The Km and Vmax for the purified enzyme with NP-palpitate were calculated to be 0.0016 mM and 0.885 mM min-1 ml-1, respectively.

The optimal activity of the enzyme was detected at pH 7.5 and 55˚ C.

Enzyme showed remarkable thermo stability, it retained 33% of its original activity at 100 ˚C for 30 minutes.

The enzyme showed no metal ion dependence for its activity since EDTA up to 15 mM had no effect on the enzyme activity.