A glycoprotein α ‐amylase inhibitor from Withania somnifera differentially inhibits various α ‐amylases and affects the growth and development of Tribolium castaneum

BACKGROUND Identification and characterisation of plant defensive molecules enrich our resources to design crop protection strategies. In particular, plant‐derived proteinaceous inhibitor(s) of insect digestive enzymes appear to be a safe, sustainable and attractive option. RESULTS A glycoprotein having non‐competitive α ‐amylase inhibitory activity with a molecular weight of 8.3 kDa was isolated and purified from seeds of Withania somnifera α ‐amylase inhibitor ( WSAI ). Its mass spectrometry analysis revealed 59% sequence coverage with Wrightide II ‐type α‐amylase inhibitor from Wrightia religiosa . A dose‐dependent inhibition of α ‐amylases from Aspergillus oryzae , Bacillus subtilis , Helicoverpa armigera and Tribolium castaneum was recorded. Interestingly, WSAI did not inhibit human salivary α ‐amylase significantly. When adults of T. castaneum were fed with WSAI (1.6 mg g −1 ), decrease in consumption, growth and efficiency of conversion of ingested food was evident, along with over fourfold increases in feeding deterrence index. A decline in larval residual α ‐amylase activity after feeding of WSAI resulted in a reduction in longevity of T. castaneum . CONCLUSION The study reflects the significance of WSAI in affecting the overall growth and development of T. castaneum . Pre‐ and post‐harvest pest resistive capability makes WSAI a potential candidate for insect pest management. Further, the effectiveness of this inhibitor could be explored either in formulations or through a transgenic approach. © 2016 Society of Chemical Industry