title: Stabilization of potato tuber lipoxygenase on talc.
abstract: Potato tuber lipoxygenase, like many plant enzymes is a very labile protein and can lose activity during or after the purification procedure. In order to overcome this problem, we immobilized potato tuber lipoxygenase by adsorption on talc, a silicate support. Lipoxygenase adsorption greatly increased the long-term stability of the enzyme without modifying enzyme specificity. Moreover, adsorption on talc could be used to purify labile enzymes whose enzymatic activity decreases rapidly during purification stages. A multi-step reaction to produce large quantities (around 100 mg) of fatty acid hydroperoxides without enzyme inactivation was developed.
authors.affiliation: U.R.A. CNRS No. 1485, Faculté de Médecine et de Pharmacie de Limoges, France.
authors.forename: S
authors.initials: S
authors.lastname: Battu
authors.forename: J
authors.initials: J
authors.lastname: Cook-Moreau
authors.forename: J L
authors.initials: JL
authors.lastname: Beneytout
mesh_terms: D000327:Adsorption; D004800:Enzymes, Immobilized; D006863:Hydrogen-Ion Concentration; D008084:Lipoxygenase / Q000737:chemistry*; D016859:Lipoxygenase Inhibitors / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D011198:Solanum tuberosum / Q000201:enzymology*; D013627:Talc / Q000737:chemistry; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D016859:Lipoxygenase Inhibitors; D010940:Plant Proteins; D013627:Talc; D008084:Lipoxygenase