The aims of this work were to study the kinetics of glutathione-S-transferase enzyme organised by Langmuir-Blodgett technique and to analyse the extent of its residual enzymatic activity also after long storage and thermal treatment. The enzyme was deposited onto activated/inactivated silicon supports by the Langmuir-Schaefer technique and enzymatic activity of the film was analysed spectrophotometrically following the glutathione conjugation to 1-chloro-2,4-dinitrobenzene, The apparent kinetic constants of Michaelis-Menten equation, i.e.,K-m and V-max, were estimated. Circular dichroism measurements on LB film were carried out to analyse the effect of high temperature exposure on the secondary structure of the enzyme in LB film.