Effectiveness of Talc as Adsorbent for Stabilization and Expression of Pisum sativum hortense Cv. Solara Lipoxygenase−Lyase Coupled Activities

Pisum sativum hortense cv. Solara lipoxygenase differs from previously described lipoxygenases by the presence, at optimum pH, of dual activities that can convert linoleic acid into two products, 9-hydroperoxyoctadecadienoic acid by a classical lipoxygenase activity and 2,4-decadienal by lyase activ...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 1996-08, Vol.44 (8), p.2057-2062
Main Authors: Liagre, Bertrand, Battu, Serge, Rigaud, Michel, Beneytout, Jean L
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
ADSORCION
ADSORPTION
ENZYME INHIBITORS
ENZYMIC ACTIVITY
ESTABILIDAD
GRAINE
IMMOBILISATION
IMMOBILIZATION
INHIBIDORES DE ENZIMAS
INHIBITEUR D'ENZYME
INMOVILIZACION
LIASAS
LIPOXIGENASA
LIPOXYGENASE
LYASE
LYASES
MINERALES
MINERALS
MINERAUX
PISUM SATIVUM
SEEDS
SEMILLA
STABILITE
STABILITY
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Summary:Pisum sativum hortense cv. Solara lipoxygenase differs from previously described lipoxygenases by the presence, at optimum pH, of dual activities that can convert linoleic acid into two products, 9-hydroperoxyoctadecadienoic acid by a classical lipoxygenase activity and 2,4-decadienal by lyase activity on an intermediate peroxyl radical. This enzyme is a very labile protein and can lose activity during or after the purification procedure. In order to overcome this inconvenience, we immobilized P. sativum lipoxygenase−lyase by adsorption on talc and we explored the evolution and stability of both activities after adsorption. For lipoxygenase or lyase activity, we obtained a specific immobilization on talc with an increase in long-term stability at 4 °C in comparison to free enzyme and especially for immobilized lyase activity (60% of activity after 30 days). Immobilized enzymes appeared to be less sensitive to inhibitors than free, but the increase in IC50 values for immobilized enzymes was in fact the result of a nonspecific adsorption of inhibitor. Therefore, despite the difference between IC50 values, free and immobilized enzyme behavior toward inhibitors were comparable. Keywords: Pisum sativum lipoxygenase−lyase; enzyme adsorption; talc
ISSN:0021-8561
1520-5118
DOI:10.1021/jf950424q