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An esterase fromBacillus 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.

applied and environmental microbiology

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

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