An efficient nanobioconjugate of lipase B from Candida antarctica was prepared by covalent binding onto carboxy-functionalized single-walled carbon nanotubes and tested in batch and flow modes for the enzymatic kinetic resolution of several racemic secondary 1-arylethan-1-ols. The influence of various process parameters such as temperature, flow rate and substrate concentration upon the biocatalyst efficiency and selectivity in the kinetic resolution of rac-1-phenylethan-1-ol was investigated and the conditions for the highest productivity were determined. The long-term activity and selectivity of the biocatalyst were preserved, enabling hundred gram scale resolution of rac-1-phenylethan-1-ol with only ∼70 mg of biocatalyst.