Sol-gel immobilized lipase from Burkholderia cepacia (Amano PS) was utilized for the first time as biocatalyst for kinetic resolution of 1,5-dihydroxy-1,2,3,4-tetrahydronaphthalene, by transesterification in batch and continuous-flow mode. The ternary silane precursor mixture of vinyltrimethoxysilane, phenyltrimethoxysilane and tetramethoxysilane, in equimolar ratio, yielded the best immobilized enzyme in terms of catalytic activity and enantiomer selectivity. Vinyl acetate was the most efficient acyl donor and proved to be the best reaction medium as well, but needing a certain amount (about 43%) of tetrahydrofuran as co-solvent to increase the solubility of the substrate: The optimal conditions determined for the kinetic resolution in the batch system were utilized for the continuous-flow process in the packed-bed reactor, too. The immobilized lipase "demonstrated excellent operational stability during a continuous 4-day experiment, preserving the productivity (r(flow)) value above 180 mu mol h(-1) g catalyst(-1) and the enantiomer selectivity (E) above 200. The (R)-selectivity of the Burkholderia cepacia in relation with this substrate was evidenced by NMR analysis. (C) 2016 Elsevier Ltd. All rights reserved.