S. Colombie et al., Irreversible lysozyme inactivation and aggregation induced by stirring: kinetic study and aggregates characterisation, BIOTECH LET, 22(4), 2000, pp. 277-283
Stirring strongly enhanced irreversible inactivation and aggregation of lys
ozyme being studied as a model enzyme. From 0 to 740 rpm (equivalent to imp
eller tip speeds from 0 to 0.77 m s(-1)), the inactivation kinetic constant
was proportional to the power imparted by the impeller. Collisions between
inactive and native molecules induced inactivation of the latter and led t
o lysozyme aggregation. These fractal aggregates of lysozyme were made of m
onomers, dimers and trimers.