Integration of membrane filtration and biocatalysis has appealing benefits in terms of simultaneous substrate conversion and product separation in one reactor. Nevertheless, the interaction between enzymes and membrane is complex and the mechanism of enzyme docking on membrane is similar to membrane fouling. In this study, focus is given on the assessment of enzyme immobilization mechanism on reverse asymmetric polymer membrane based on the permeate flux data during the procedure. Evaluation of membrane performance in terms of its permeability, fouling mechanisms, enzyme loading, enzyme reusability and biocatalytic productivity were also conducted. Alcohol Dehydrogenase (EC 220.127.116.11), able to catalyze formaldehyde to methanol with subsequent oxidation of NADH to NAD was selected as the model enzyme. Two commercial, asymmetric, flat sheet polymer membranes (PES and PVDF) were immobilized with the enzyme in the reverse mode. Combination of concentration polarization phenomenon and pressure driven filtration successfully immobilized almost 100% of the enzymes in the feed solutions. The biocatalytic membrane reactor recorded more than 90% conversion, stable permeate flux with no enzyme leaching even after 5 cycles. The technique showing promising results to be expanded to continuous membrane separation setup for repeated use of enzymes.