Glycoprotein alpha-amylase inhibitor from Withania somnifera differentially inhibits various alpha-amylases and affects the growth and development of Tribolium castaneum

TitleGlycoprotein alpha-amylase inhibitor from Withania somnifera differentially inhibits various alpha-amylases and affects the growth and development of Tribolium castaneum
Publication TypeJournal Article
Year of Publication2017
AuthorsKasar, SS, Marathe, KR, Bhide, AJ, Herwade, AP, Giri, AP, Maheshwari, VL, Pawar, PK
JournalPEST Management Science
Volume73
Issue7
Pagination1382-1390
Date PublishedJUL
Type of ArticleArticle
Abstract

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 alpha-amylase inhibitory activity with a molecular weight of 8.3 kDa was isolated and purified from seeds of Withania somnifera alpha-amylase inhibitor (WSAI). Its mass spectrometry analysis revealed 59% sequence coverage with Wrightide II-type alpha-amylase inhibitor from Wrightia religiosa. A dose-dependent inhibition of alpha-amylases from Aspergillus oryzae, Bacillus subtilis, Helicoverpa armigera and Tribolium castaneumwas recorded. Interestingly, WSAI did not inhibit human salivary alpha-amylase significantly. When adults of T. castaneum were fed with WSAI (1.6mg g(-1)), decrease inconsumption, growthandefficiency of conversion of ingested foodwas evident, along withover fourfold increases in feedingdeterrence index. Adecline inlarval residual alpha-amylase activity after feedingofWSAI resulted ina 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. (C) 2016 Society of Chemical Industry

DOI10.1002/ps.4467
Type of Journal (Indian or Foreign)

Foreign

Impact Factor (IF)

2.811

Divison category: 
Biochemical Sciences

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