@article { ISI:000310401100058,
	title = {Inhibition of xyloglucanase from an alkalothermophilic thermomonospora sp by a peptidic aspartic protease inhibitor from Penicillium sp VM24},
	journal = {Bioresource Technology},
	volume = {123},
	year = {2012},
	month = {NOV},
	pages = {390-399},
	publisher = {ELSEVIER SCI LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<p>A bifunctional inhibitor from Penicilliurn sp VM24 causing inactivation of xyloglucanase from Thermomonospora sp and an aspartic protease from Aspergillus saitoi was identified. Steady state kinetics studies of xyloglucanase and the inhibitor revealed an irreversible, non-competitive, two-step inhibition mechanism with IC50 and K-i; values of 780 and 500 nM respectively. The interaction of o-phthalaldehyde (OPTA)-labeled xyloglucanase with the inhibitor revealed that the inhibitor binds to the active site of the enzyme. Far- and near-UV spectrophotometric analysis suggests that the conformational changes induced in xyloglucanase by the inhibitor may be due to irreversible denaturation of enzyme. The bifunctional inhibitor may have potential as a biocontrol agent for the protection of plants against phytopathogenic fungi. (C) 2012 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Aspartic protease, Bifunctional inhibitor, Biocontrol agent, Inactivation mechanism, Xyloglucanase},
	issn = {0960-8524},
	doi = {10.1016/j.biortech.2012.07.050},
	author = {Menon, Vishnu and Rao, Mala}
}
@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.}
}
