Characterization of wheat germ lipase

Some properties of wheat germ lipase were determined with a fluorometric assay of enzymatic cleavage converting the nonfluorescent 4-methyl umbelliferone butyrate (4-MUB) to the highly fluorescent 4-methyl umbelliferone (4-MU). Optimum reaction conditions were attained at buffer pH 7·5 and temperature 30°. Lineweaver-Burk plots were linear. Relative cation combination effectiveness as reaction activators was Ca + Mg + K > Ca + Mg + K + Na > Ca + Mg + Na > Ca + Mg > Mg > Ca, with no reaction effects of K, Na, and K + Na without Ca or Mg. Highly significant inhibitors of lipase reaction were CN⁻, aflatoxin, Cu²⁺, Fe³⁺, S²⁻, and EDTA.