title: One-Step Purification of a Lipolytic Enzyme from Bacillus pumilus by Mild Hydrophobic Interaction Chromatography on Polyoxyalkylene Glycol-Bound Sepharose 6B.
abstract: 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.
authors.affiliation: Laboratoire de Chimie-Physique Macromoléculaire, Ecole Nationale Supérieure des Industries Chimiques, 1, Rue Grandville, 54042 Nancy Cedex, and Laboratoire de Microbiologie, Ecole Supérieure des Sciences et Technologies des Industries du Bois, Université de Nancy I, 54506 Vandoeuvre-lés-Nancy Cedex, France.
authors.forename: R
authors.initials: R
authors.lastname: Mathis
authors.forename: A
authors.initials: A
authors.lastname: Mourey
authors.forename: P
authors.initials: P
authors.lastname: Hubert