• digestive lipase;
  • Pieris brassicae;
  • host plant;
  • inhibitor

The properties of a digestive lipase from the larval midgut of Pieris brassicae were studied by performing biochemical purification, characterization, effect of host plants, and extracted inhibitors. The purification process revealed a lipase with a purification fold of 42, recovery of 18.12%, molecular weight mass of 72.3 kDa, optimal pH at 11, and optimal temperature at 30°C, as well as stability at the optimal temperature for 12 h. The purified enzyme was inhibited by the ions Na+, Mn+, Fe2+, and Cu2+ and the inhibitors SDS, EDTA, TTHA, and mercaptoethanol. Ca2+ and Mg2+ increased activity of the purified lipase, but urea, PMSF, EGTA, and DTC had no effect on enzymatic activity. Feeding of larvae on three host plants, Trepaeolus majus, Brassica olearcea var. alba, and B. olearcea var. rubra revealed the highest lipase activity on T. majus, but the two varieties of B. olearcea significantly decreased lipase activity. Extraction of a crude inhibitor from two varieties of B. olearcea demonstrated that the crude inhibitor inhibited the purified lipase up to 75%. The inhibitor changed the kinetic parameters of the enzyme by elevating the Km, as in competitive inhibition. The data suggest a possible role for plant lipase inhibitors in host plant resistance.