In this work, the immobilization of two hydrolases on plasma-modified polypropylene carriers was investigated. Treating Accurel MP1001 with an oxygen plasma was found most suitable to increase the hydrophilicity and to allow for efficient immobilization. Thus, for lipase B from Candida antarctica and for an esterase from Pyrobaculum calidifontis esterase (PestE) a 5-fold and 14-fold increase, respectively, in immobilization yield resulted compared to untreated carrier. In contrast to the oxygen-modified support, modification of the polypropylene carrier with ammonia plasma showed no positive effect. Furthermore, it could be shown that immobilized PestE catalyzed enantioselective transesterification of α-phenylethanol in vinyl acetate, whereas the free enzyme showed no activity. Both hydrolases could be recycled five times without significant loss of activity.