One-Step Purification of a Lipolytic Enzyme from Bacillus pumilus by Mild Hydrophobic Interaction Chromatography on Polyoxyalkylene Glycol-Bound Sepharose 6B.

An esterase from Bacillus pumilus was obtained in a highly purified form, starting from a crude extract, by a new chromatographic technique requiring no detergent during the elution step. The stationary phase involved was mildly hydrophobic and was prepared by covalent immobilization of a polyoxyalkylene glycol onto Sepharose 6B.