The present work investigates the reaction kinetics of immobilised lipase esterification of oleic acid and octanol, in a solvent-free system. Lipase from Rhizomucor miehei was immobilised on a hydrophobic support. The initial reaction rate was investigated as a function of octanol concentration and temperature, and the reaction kinetics were described in terms of the Michaelis-Menten mechanism. Evaluating K-m, V-max and k(cat)/K-m as a function of temperature, it was found that K-m was minimum and k(cat)/K-m was maximum at 40 degrees C while V-max was maximum at 50 degrees C. Furthermore, applying the Ping Pong Bi Bi mechanism yielded good results for this two-substrate system.