KINETIC CHARACTERIZATION OF PENICILLIUM-CITRINUM LIPASE IN AOT ISOOCTANE-REVERSED MICELLES/

A lipase from a wild strain of Penicillium citrinum was encapsulated i n AOT/isooctane-reversed micelles, and the kinetic parameters were stu died relative to triolein hydrolysis. Lipolytic activity was strongly dependent on the water amount in the system (W-o) and presented a bell -shaped curve for this parameter, with a maximum in the range of W-o 1 0-15. Optimum conditions for enzyme activity were pH 8.0 and 45 degree s C. The influence of substrate concentration was also studied. The en zyme showed a Michaelis-Menten behavior and the apparent kinetics cons tants were calculated as being V-max.app. = 120 U/mg and K-mapp = 49.2 mM.