A method for entrapment of enzymes within an inorganic matrix was developed using a sol-gel process. Such entrapping immobilization of biocatalysts within inorganic matrices has some benefits but it is rather difficult to apply in contrast to other types of immobilization and therefore has not been commercialized. The method developed was applied to entrapping lipase within silica beads. The entrapped lipase was six times more active for esterification in an organic medium than lipase immobilized over silica glass with a binding method which has conventionally been used. The high activity may come from the characteristics of the present method. It can entrap the enzyme with less denaturation and provide the matrix with physical properties suited to the reaction, e.g. an abumolance of macro pores.