Enhanced production of hydroperoxides by immobilized lipoxygenase in the presence of cyclodextrins.
The advantages of the presence of cyclodextrins in a reaction catalyzed by immobilized lipoxygenase at neutral pH are reported for the first time. The steady-state rate in the presence of beta-cyclodextrins was seven times higher than in control experiments using the same concentration of linoleic acid; furthermore the percentage of substrate conversion (and product accumulation) obtained in the presence of beta-cyclodextrins was higher than in the control assays. The optimum concentration of free linoleic acid coincided with the critical micellar concentration for linoleic acid at neutral pH. The operational stability of the immobilized enzyme increased in the presence of beta-cyclodextins, while an increase in the percentage of 13-HPOD was also observed.
Pérez-Gilabert
Manuela
M
Departamento de Bioquímica y Biología Molecular-A, Universidad de Murcia, Espinardo 30071, Spain. mpg@um.es
García-Carmona
Francisco
F
D001709:Biotechnology; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D007700:Kinetics; D008054:Lipid Peroxides / Q000032:analysis / Q000096:biosynthesis*; D008084:Lipoxygenase / Q000378:metabolism*; D011108:Polymers; D013025:Glycine max / Q000201:enzymology; D047392:beta-Cyclodextrins
D004800:Enzymes, Immobilized; D008054:Lipid Peroxides; D011108:Polymers; D047392:beta-Cyclodextrins; C065843:Eupergit C; D008084:Lipoxygenase