Expression, purification and enzymatic properties of a beta-N-acetylhexosaminidase from brown planthopper, Nilaparvata lugens

作者：Zhang, Yunhua; Ji, Jinyun; Zhao, Xiao; Jin, Ruoheng; Li, Jianhong; Wan, Hu^*

来源：Journal of Asia-Pacific Entomology, 2017, 20(4): 1340-1343.

DOI：10.1016/j.aspen.2017.10.005

• beta-N-acetyl-D-hexosaminidase
• Enzymatic activity
• pH
• Temperature
• Inhibition
• Nilaparvata lugens

A previous study demonstrated that a beta-N-acetyl-D-hexosaminidase (NIHex4) from the brown planthopper could serve as a new potential target for biopesticides due to its requirement for molting, and lethal phenotypes were observed via RNA interference. However, the enzymatic properties of NIHex4 remain unclear. In the present study, NIHex4 was expressed, purified and characterized. Recombinant NIHex4 was functionally expressed in baculovirus-infected insect cells and purified with a molecular weight of approximately 70 kDa. Recombinant NIHex4 had an optimal pH and temperature of 6.0 and 60 degrees C, respectively. Moreover, recombinant NIHex4 exhibited thermal stability at 50 degrees C for at least 1 h. Furthermore, the activity of recombinant NIHex4 was inhibited by the metal ions Fe2+ and Fe3+ and the serine protease inhibitor phenylmethanesulfonyl fluoride. These results reveal the enzymatic properties of NIHex4 and provide a basis for future investigation of the interaction between HEX and chitin oligosaccharide.

• 出版日期2017-12
• 单位华中农业大学