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Expression, purification and binding characteristics of general odorant binding protein I (GOBP1) from the meadow moth, Loxostege sticticalia (Linnaeus) (Lepidoptera: Pyralididae)
Odorant-binding proteins (OBPs) are responsible for physiological function via perception of volatile odors. Here we reported the successful expression and purification of a general odorant binding protein Lsti-GOBPl from Loxostege sticticalis L. Lsti-GOBPl was expressed using Escherichia coli Rosetta (DE3) prokaryotic expression system, and then purified using Histrap HP column, and the protein functions of Lsti-GOBPl were tested by fluorescent probe N-phenyl-1-naphthylamine (1-NPN) binding assays and competitive binding assays with 50 kinds of chemical molecules. The results showed that Lsti-GOBPl had the capability of binding 35 odorants. However, only 1-hexanol, 1-heptanol, cinnamaldehyde and camphene replaced 1-NPN from Lsti-GOBPl by 50%, and their binding constants were 8.997, 7.283, 7.289 and 9.814 mu nol/L, respectively. So, it can be speculated that Lsti-GOBPl has a wide binding characteristics, but it has strong binding specificity to 1-hexanol, 1-heptanol, cinnamaldehyde and camphene, which probabl