Surfactant-coated lipase (SCL) was prepared by coating the surface of Candida cylindracea lipase with the non-ionic surfactant, Span 85. SCL catalyzed the esterification of geraniol and acetic acid. The ester product, geranyl acetate, is an important component of flavor and fragrance compounds. The SCL prepared in this work had low solubility in organic solvent, unlike those prepared by other investigators. A kinetic study of the mechanism of the lipolytic esterification and the reaction rate for facilitating the scale-up of the reactors indicated a ping-pong bi bi model with competitive substrate inhibition by acetic acid and dead-end inhibition by acetic acid. Experimental data agreed with the proposed model. Kinetic parameters, K-i, K-m(AA), K-m(GOH) and V-max, were determined which visualized the reaction mechanism of the SCL esterification.