Journal
PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY
Volume 163, Issue -, Pages 227-234Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pestbp.2019.11.022
Keywords
Carboxylesterase; Odorant-degrading enzyme; Spodoptera exigua; Ubiquitous expression
Categories
Funding
- National Natural Science Foundation of China [31860617, 31360528, 31401750]
- Natural Science Foundation of Guihou Province of China [QKH-J [2019]1109]
- talented people of Guizhou QKH platform [[2017]5788]
- Scientific Research Foundation of Guizhou University of China (RJH Project) [2013-28, 2017-33]
- Major Program of Innovation Research Team of Educational Commission of Guizhou Province of China [QJH-KY[2016]113]
- Science and Technology Platform for Talent of Guizhou Province [QKH [2016]5608]
- Technical Cooperation Project of Food and Agriculture Organization of United Nations [TCP/CPR/3603]
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Odorant-degrading enzymes (ODEs) are considered to play key roles in odorant inactivation to maintain the odorant receptor sensitivity of insects. Some members of carboxylesterase (CXE) is a major sub-family of ODEs. However, only a few CXEs have been functionally characterized so far. In the present study, we cloned the antennal esterase SexiCXE11 cDNA full-length sequences from the male antennae of a notorious crop pest, Spodoptera exigua, and its encoded 538 amino acids. It was similar to other insect esterases and had the characteristics of a carboxylesterase. We expressed recombinant enzyme in High-Five insect cells and obtained the high level purified recombinant protein by affinity column. Furthermore we test enzyme activity toward its two acetate sex pheromone components (Z9,E12-Tetradecadienyl acetate, Z9E12-14:Ac and Z9-Tetradecenyl acetate, Z9-14:Ac) and other 18 ester plant volatiles. Our results demonstrated that SexiCXE11 degraded acetate sex pheromone components with similar degradation activities (about 15.75% with Z9E12-14:Ac and 19.28% with Z9-14:Ac) and plant volatiles with a relatively high activity such as pentyl acetate and (Z)-3-hexenyl caproate. SexiCXE11 had high hydrolytic activity with these two ester odorants ( > 50% degradation), which is characterized that although a ubiquitous expression esterase SexiCXE11 may be partly involved with olfaction. This study may facilitate a better understanding of moth ODE differentiation and suggest strategies for the development of new pest behavior inhibitors.
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