AthenaES™ Specialty Proteins

Bacterial Esterases and Lipases

Vials of bacterial esterases LypA, TesA, and VlpA.
  • Broad spectrum of substrate activity
  • Flexible solvent tolerant structure
  • Stereoselective
Enzyme EC Class Source Special Properties
TesA EC thioesterase from E. coli Mesophilic, Substrates: diacyl glycerides, acyl-thioesters, and r-nitrophenyl esters
LypA EC lysophospholiopase L2 from Vibrio cholera Mesophilic, Substrates: diacyl glycerides and r-nitrophenyl esters, poor thioesterase activity
VlpA EC lipase from a marine Vibrio sp. Psychrophilic, Substrates: broad activity with short and long chain acryl esters, solvent tolerant
Cold-tolerant bacterial esterases and lipases have the unusual property of a flexible structure which allows these enzymes to accommodate a broad range of substrates and to be more solvent tolerant. These properties coupled with the stereoselectivity of enzymes, make esterases and lipases ideal catalysts for the chemical modification of pharmacophore molecules. Employing an array of techniques to identify esterase/lipase activity for industrial processes, an in-house microbial collection of psychrophilic microbes was used to screen for specific esterase/lipase activities. Two marine bacteria yielded esterase/lipase genes encoding LypA (V. cholera) and VlpA (artic-derived Vibro sp.). These enzymes have broad spectrum substrate activity and VlpA exhibits tolerance to solvents by retaining its catalytic activity in buffer-solvent mixtures.
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0305-1 LypA 100 units $345.00
0305-5 LypA 500 units $1,537.00
0306-1 TesA 100 units $345.00
0306-5 TesA 500 units $1,537.00
0307-1 VlpA 100 units $402.00
0307-5 VlpA 500 units $1,793.00
VlpA exhibits tolerance to the solvent (DMSO) by retaining its catalytic activity in buffer-solvent mixtures.
The graph above shows the solvent tolerance of VlpA in di-methyl-sulfoxide (DMSO). VlpA (2 units) was reacted with 100µmoles p- nitrophenyl butyrate in 50mM Tris-Cl pH 9.0 in the presence of different amounts of DMSO. The initial reaction rates were measured and the percent activity relative to the "no solvent" control calculated. VlpA exhibits tolerance to the solvent by retaining its catalytic activity in buffer- solvent mixtures.