PMC

Phylogenetic tree showing the genetic relationship between SG2 lipase and the other Family I lipases EF434173 - B. pumilus XJU-13 lipase; AF232707 - Bacillus sp. B26 lipase; EU414610 - B. licheniformis RSP - 09 lipase; EF093106 - B. pumilus F3 lipase precursor; AY494714 - B. pumilus lipase precursor; EU482152 - B. pumilus B106 lipase (lipA); FM878604 - B. pumilus triacylglycerol lipase; DQ339137 - B. pumilus YZ02 lipase; DQ345448 - B. pumilus mutant lipase precursor; EU552794 - B. pumilus strain GMA1 lipase precursor; FJ544454 - B. subtilis lipase (lipW); AE017333 - B. licheniformis DSM13; FJ467614 - B. pumilus HZbp lipase; AB244464 - B. cereus C7-2; AF134840 - B. thermoleovorans lipase (ARA); AY634688 - B. coagulans strain 81-11 carboxylesterase; AJ430831 - B. megaterium lipA extracellular esterase; AJ430985 - Bacillus sp. BP-6 lipA extracellular esterase; FJ601712 - Synthetic construct clone JK lipM1 triacylglycerol lipase.

The lipase BT-1 incubated in in 50 mM Tris-HCl buffer (pH 8) at various temperatures (4-70°C) and assayed for lipase activity. B. Effect of pH on the activity of lipase BT-1. The lipase BT-1 incubated in various buffer (pH 2.2-11.0) at 25°C and assayed for lipase activity.

(a) AFB1 degradation by commercial lipase enzyme without inhibitor HgCl₂ during 1 h of incubation. The values are means of triplicates and the error bars represent the corresponding deviations. (b) AFB1 degradation by commercial lipase enzyme in the presence of HgCl₂, with 1 h of incubation. The values are means of triplicates and the error bars represent the corresponding deviations. (c) Silica gel Thin-layer chromatogram of aflatoxin B1 after incubation for 1 h in the presence of commercial lipase (1) Standard AFB1 (2) AFB1+ lipase (50 μg/ml) (3) AFB1+ lipase (100 μg/ml) (4) AFB1+ lipase (200 μg/ml) (5) AFB1+ lipase (300 μg/ml). (d) Silica gel Thin-layer chromatogram of aflatoxin B1after incubation for 1 h in the presence of Commercial lipase and HgCl₂ (6.4 μg/ml). (1) Standard AFB1 (2) AFB1+ Commercial lipase (100 μg/ml)+HgCl₂ (3) AFB1+ Commercial lipase (200 μg/ml)+HgCl₂ (4) AFB1+Commercial lipase (300 μg/ml)+HgCl₂ (5) AFB1+Commercial lipase (in sequence from left to right).

Blocks of sequences conserved in the LipR cluster of putative bacterial lipases assigned to bacterial lipase family X. The aligned sequences were the putative lipases forming the LipR cluster. YP_002769179, putative lipase from R. erythropolis PR4; ZP_04383612, putative triacylglycerol lipase from R. erythropolis SK121; YP_345621, putative lipase from R. erythropolis PR4; ZP_04386725, triacylglycerol lipase from R. erythropolis SK121; ZP_07281779, putative triacylglycerol lipase from Streptomyces sp. strain AA4; ZP_06908675, putative triacylglycerol lipase from S. pristinaespiralis ATCC 25486; ZP_04693904, putative lipase from S. roseosporus NRRL 15998; YP_003111889, putative triacylglycerol lipase from Catenulispora acidiphila DSM 44928; ZP_07716111, putative triacylglycerol lipase from Aeromicrobium marinum DSM 15272; YP_002235365, putative exported lipase from Burkholderia cenocepacia J2315; ZP_04942934, putative triacylglycerol lipase from B. cenocepacia PC184; YP_625098, putative triacylglycerol lipase from B. cenocepacia AU 1054; YP_001778248, putative triacylglycerol lipase from B. cenocepacia MC0-3; YP_370846, putative triacylglycerol lipase from Burkholderia sp. strain 383. ZP_07149178, putative triacylglycerol lipase from Corynebacterium resistens DSM 45100; YP_119470, putative lipase from Nocardia farcinica IFM 10152. The amino acids constituting the conserved pentapeptide are underlined. Alignment was performed with the web tool MAFFT. Identical amino acids are on a black background, whereas a gray background indicates identical or equivalent amino acids.