Plant lectins have displayed a variety of biological activities. In this study, for the first time, a 27 kDa arabinose-and mannose-specific lectin from Broccolini (Brassica oleracea Italica x Alboglabra), named as BL (Broccolini lectin), was purified by an activity-driven protocol. Mass spectrometry analysis and database search indicated that no matches with any plant lectin were found, but BL contained some peptide fragments (QQQGQQGQQLQQVISR, QQGQQQGQQGQQLQQVISR and VCNIPQVSVCPF QK). BL exhibited hemagglutinating activity against chicken erythrocytes at 4 mu g/mL. BL retained full hemagglutinating activity at pH 7-8 and temperature 30-40 degrees C, and had an optimal activity in Ca2+ solution. Bioactivity assay revealed that BL exhibited dose-dependent inhibition activity on 5 bacterial species with IC50 values of 143.95-486.33 mu g/mL, and on 3 cancer cells with IC50 values of 178.82-350.93 mu g/mL. Notably, 5-fold reduction in IC50 values was observed on normal L-O2 vs cancerous HepG-2 cells (924.35 vs. 178.82 mu g/mL). This suggests that BL should be promising in food and medicine. (C) 2015 American Institute of Chemical Engineers