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Stabilization of potato tuber lipoxygenase on talc
S Battu1, J Cook-Moreau, J L Beneytout
1U.R.A. CNRS No. 1485, Faculté de Médecine et de Pharmacie de Limoges, France.
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.

