Alpha-l-rhamnosidase activity in non-aqueous solvent systems

Abstract

Enzymes are highly specific catalysts that typically function in aqueous solvents. However, many enzymes retain their catalytic activities at high concentrations in non-aqueous environments. Non-aqueous biocatalysis is suitable for synthesis of commercially important pharmaceutical precursors and drugs, such as pure enantiomers, chiral molecules, single isomers and biopolymers. a-L-Rhamnosidase (EC 3.2.1.40) was partially purified from Brevundimonas sp. Ci19 intracellular extracts by ultrafiltration and gel-filtration chromatography with a performance of 27-fold purification. a-L-Rhamnosidase displayed high activity in 20% solvent (dimethylsulfoxide, ethylenglycol, glycerol, methanol, 2-propanol, and propilenglycol) at 30 ºC. Especially in the case of DMSO and 2-Propanol solutions, enzymatic activity was higher compared to aqueous system. The a-L-rhamnosidase produced by the psychrotolerant bacterial strainBrevundimonas sp. Ci19 showed interesting properties and could be used in industrial processes containing organic solvents mixtures.