GmolCXEs degraded free ester sex pheromone components in mating
We firstly expressed GmolCXE1 and GmolCXE5 proteins using E. coliTransetta (DE3) cells. Then we purified proteins by Ni ion affinity
chromatography (Figure S3). The sex pheromone mixtures were incubated
with each purified esterase protein for 1 h before submitted to EAG
analysis. As shown in Figure 5, the antennae of male moths had a strong
EAG responses to these two ester sex pheromone compounds
Z8-12:Ac, E8-12:Ac, and mix
(Z8-12:Ac: E8-12:Ac=9:1) under normal conditions. However, after
incubated with the purified GmolCXE1 or GmolCXE5 proteins, the EAG
amplitudes in response to sex pheromone compounds Z8-12:Ac, E8-12:Ac,
and mix were significantly reduced in male moths (Figure 5 A-C).
GC-MS results showed that after Z/E8-12:Ac treated with GmolCXE1 or
GmolCXE5, the metabolites Z/E8-12:OH were detected (Figure 6 A-C and
E-G). And degradation percentage of Z8-12:Ac were 100% (CXE1) and
35.52% (CXE5) (Figure 6D), and degradation percentage of E8-12:Ac were
64.99% (CXE1) and 33.23% (CXE5) (Figure 6 H).