Stabilization of potato tuber lipoxygenase on talc.
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.
Battu
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U.R.A. CNRS No. 1485, Faculté de Médecine et de Pharmacie de Limoges, France.
Cook-Moreau
J
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Beneytout
J L
JL
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
D004800:Enzymes, Immobilized; D016859:Lipoxygenase Inhibitors; D010940:Plant Proteins; D013627:Talc; D008084:Lipoxygenase