@article {49511,
	title = {Novel bifunctional inhibitor of protease and α-amylase from Clitorea ternatea restricts the growth and development in Spodoptera frugiperda},
	journal = {International Journal of Biological Macromolecules},
	volume = {305},
	year = {2025},
	month = {MAY},
	pages = {141180},
	type = {Article},
	abstract = {<p>
	An inhibitor molecule capable of inhibiting a wide range of digestive enzymes without affecting endogenous enzymes is always desirable. We report characterization of CteTAI (M.W. 14 kDa), a bifunctional inhibitor (BFI) protein from the seeds of Clitoria ternatea capable of inhibiting trypsin and alpha-amylase. It retains trypsin inhibition activity up to 60 degrees C and alpha-amylase inhibition up to 40 degrees C. Trypsin inhibition is stable across pH 1-12, while alpha-amylase inhibition is stable between pH 3-7. CteTAI is a noncompetitive inhibitor of trypsin and an uncompetitive inhibitor of alpha-amylase. It selectively inhibits proteases and alpha-amylases from various sources, without affecting alpha-amylase from human saliva and Bacillus spp. Proteomic analysis identified CteTAI as a bifunctional inhibitor exhibiting 41 \% similarity to a bifunctional inhibitor from Sesbania bispinosa. Feeding Spodoptera frugiperda larvae with CteTAI-infused diet impaired energy metabolism, resulting in undernourished larvae and malformed adults incapable of flight and mating. Key nutritional indices (RGR, RCR, \%ECI, \%FDI) were severely reduced, indicating that CteTAI disrupts growth and development by inhibiting multiple protease and alpha-amylase isoforms. Biochemical characterization of newly identified CteTAI suggests its potential application in crop protection.</p>
},
	keywords = {alpha-Amylase inhibitors, Bifunctional inhibitor, Clitoria ternatea, Protease inhibitors, Spodoptera frugiperda},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2025.141180},
	author = {Dongare, Pratiksha M. and Madage, Varsha A. and Deshpande, V. Neha and Joshi, Rakesh S. and Giri, Ashok P. and Pawar, Pankaj K.}
}
