Stability and catalytic kinetics of protease loaded liposomes

The purpose of this study was to prepare liposomes through Mozafari method to encapsulate Flavourzyme as the flavor-enhancing enzyme at cheese ripening. Some kinetic parameters of encapsulated protease were determined and compared with corresponding free enzyme. Kinetic studies indicated an increase in both Michaelis–Menten constant and maximum velocity in encapsulated Flavourzyme. Optimum incubation temperature and pH of encapsulated enzyme did not show any significant difference with the free one. Evaluation of the thermal stability (at 35, 45 and 55 °C) shows that encapsulated enzyme was stable at 35 °C during in 6 h. Also decreased stability of encapsulated enzyme has been observed at 65 and 75 °C in 1 h. The results show increase of stability of encapsulated enzymes in pHs 7 and 8 (7 h), while it was decreased in acidic condition. Results indicate the gradually fulfilling proteolysis of casein by liposomal loaded Flavourzyme in comparison with the free enzyme.

► Liposomes prepared by Mozafari method were used for encapsulation of Flavourzyme.
► Kinetic parameters of free and encapsulated Flavourzyme were compared.
► Optimum incubation condition and stability of encapsulated enzyme were studied.
► Proteolysis trend in recombined milk containing enzyme was comprised.
► A gradually fulfilling proteolysis of casein by liposomal enzyme was observed.