Profiling substrate specificity of Lecitase Ultra to different kinds of phospholipids using monolayer technology

Substrate specificity is a crucial parameter while characterizing an enzyme, which is directly related to the potential of its application. The commercial Lecitase Ultra has been widely used in the oil degumming process to specifically hydrolyze the phospholipids present in the crude oil, but its specificity for various phospholipids still remains elusive. In the present study, selectivity of Lecitase Ultra to different kinds of phospholipids was characterized under different surface pressure condition by using monolayer technology. Hydrolytic activity of Lecitase Ultra on various phospholipids was highly dependent on the surface pressure of monolayer film. Under the same surface pressure of 25 mN m⁻¹ applied on the liquid condensed state of all the phospholipids’ monolayer films, the preference order of Lecitase Ultra to different monomolecular phospholipid film was PE > CL > PS > PI > PC. No hydrolytic activity was observed for sphingomyelin within the range of surface pressure tested. The present study provides basic information on the order of selective preference of Lecitase Ultra for various phospholipids which was not known previously, and provides additional information for better utilization of this enzyme in the oil industry. Practical applications: To the best of our knowledge, we have reported the application of monolayer technology to study the substrate selectivity of Lecitase Ultra to various natural phospholipids. This study contributes directly to applications of this enzyme in industries. Further, we try to prove that monolayer technology is very effective and simple for evaluating the enzymatic activity to some natural substrates, and should make greater contribution in the interfacial enzyme engineering field. Characterization on interfacial catalytic properties of Lecitase Ultra to different kinds of phospholipids using monolayer technique.