01772nas a2200217   4500008004100000022001400041245014500055210006900200260009900269300001200368490000800380520088800388653002201276653002701298653002101325653002701346653001801373100001801391700001401409856013101423       2012                        eng d  a0960-852400aInhibition of xyloglucanase from an alkalothermophilic thermomonospora sp by a peptidic aspartic protease inhibitor from Penicillium sp VM240 aInhibition of xyloglucanase from an alkalothermophilic thermomon  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcNOV  a390-3990 v1233 a<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>10aAspartic protease10aBifunctional inhibitor10aBiocontrol agent10aInactivation mechanism10aXyloglucanase1 aMenon, Vishnu1 aRao, Mala  uhttps://library.ncl.res.in/content/inhibition-xyloglucanase-alkalothermophilic-thermomonospora-sp-peptidic-aspartic-protease-002356nas a2200265   4500008004100000022001400041245014500055210007000200260000800270300001100278490000800289520139600297653002901693653002701722653002201749653002401771653002601795100002701821700002301848700002001871700002201891700002001913700002201933856013501955       2025                        eng d  a0141-813000aNovel bifunctional inhibitor of protease and α-amylase from Clitorea ternatea restricts the growth and development in Spodoptera frugiperda0 aNovel bifunctional inhibitor of protease and αamylase from Clito  cMAY  a1411800 v3053 a<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>
10aalpha-Amylase inhibitors10aBifunctional inhibitor10aClitoria ternatea10aProtease inhibitors10aSpodoptera frugiperda1 aDongare, Pratiksha, M.1 aMadage, Varsha, A.1 aDeshpande, Neha1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aPawar, Pankaj, K.  uhttps://library.ncl.res.in/content/novel-bifunctional-inhibitor-protease-and-%CE%B1-amylase-clitorea-ternatea-restricts-growth-and