02134nas a2200265   4500008004100000022001400041245013000055210006900185260007900254300001200333490000800345520113900353653002701492653001401519653001601533653002601549653003201575653001601607100002501623700002801648700002301676700002001699700002001719856012901739       2005                        eng d  a1096-495900aUnraveling biochemical properties of cockroach (Periplaneta americana) proteinases with a gel X-ray film contact print method0 aUnraveling biochemical properties of cockroach Periplaneta ameri  a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcJUL  a261-2660 v1413 a<p>Eleven proteinase activity bands were detected in American cockroach (Periplaneta americana) gut. These were partially purified and characterized using a gel X-ray film contact print method. Cockroach gut proteinases (CGPs) show activity over a broad range of pH with maximum activity between pH 6 and 10, and optimal activity at 50-70 degrees C. CGPs were partially purified by preparative gel electrophoresis and analyzed using synthetic substrates and inhibitors. Four of the proteases exhibited chymotrypsin-like (C1 to C4) activity and seven trypsin-like (T I to T7) activity. Accuracy of the gel X-ray film contact print method is confirmed by including bovine chymotrypsin in CGP analysis. Inhibition of CGPs with different plant proteinaceous proteinase inhibitors allowed identification of potential CGP inhibitors. Our results imply that presence of several CGP activity bands, and their stability and activity over a broad pH and temperature range might contribute to adaptation of P americana to extreme environmental conditions and the polyphagous nature of the species. (c) 2005 Elsevier Inc. All rights reserved.</p>10aactivity visualization10acockroach10agut enzymes10aPeriplaneta americana10aplant proteinase inhibitors10aProteinases1 aHivrale, Vandana, K.1 aChougule, Nanasaheb, P.1 aChhabda, Pavan, J.1 aGiri, Ashok, P.1 aKachole, M., S.  uhttps://library.ncl.res.in/content/unraveling-biochemical-properties-cockroach-periplaneta-americana-proteinases-gel-x-ray-002457nas a2200253   4500008004100000022001400041245017200055210006900227260006700296300001400363490000700377520145800384653002301842653002301865653001301888653002901901653002301930100002501953700002801978700002002006700002302026700003002049856012402079       2011                        eng d  a0022-514200aBiochemical characterisation of alpha-amylase inhibitors from achyranthes aspera and their interactions with digestive amylases of coleopteran and lepidopteran insects0 aBiochemical characterisation of alphaamylase inhibitors from ach  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcAUG  a1773-17800 v913 a<p>BACKGROUND: Starchy seeds are an important food and a source of dietary ingredients in many countries. However, they suffer from extensive predation by bruchids (weevils) and other pests. alpha-Amylase inhibitors are attractive candidates for the control of seed weevils, as these insects are highly dependent on starch as an energy source. RESULTS: A proteinaceous alpha-amylase inhibitor from the seeds of Achyranthes aspera was identified, purified and characterised. In electrophoretic analysis, two prominent amylase inhibitor activity bands (AI1 and AI2) were detected. The inhibitor was purified 9.99-fold with 1206.95 total amylase inhibitor units mg(-1) protein. The molecular weight of the purified inhibitor was around 6 kDa. The isolated alpha-amylase inhibitor was found to be resistant to heat and proteolysis. Feeding analysis of Callosobruchus maculatus larvae on a diet containing seed powder of A. aspera revealed that survival of the larvae was severely affected, with the highest mortality rate occurring on the fifth day of feeding. The isolated inhibitor inhibited the majority of amylase isoforms of C. maculatus, Tribolium confusum and Helicoverpa armigera in electrophoretic analysis and solution assays. CONCLUSION: The information obtained in the present investigation could be useful for a genetic engineering approach that would make seeds resistant to storage pest infestations. (C) 2011 Society of Chemical Industry</p>10aAchyranthes aspera10aAmylase inhibitors10aamylases10aCallosobruchus maculatus10aTribolium confusum1 aHivrale, Vandana, K.1 aChougule, Nanasaheb, P.1 aGiri, Ashok, P.1 aChhabda, Pavan, J.1 aKachole, Andmanvendra, S.  uhttps://library.ncl.res.in/content/biochemical-characterisation-alpha-amylase-inhibitors-achyranthes-aspera-and-their-002032nas a2200181   4500008004100000022001400041245013500055210006900190260009100259300001100350490000600361520125800367100002801625700002301653700002001676700002501696856012901721       2013                        eng d  a1932-620300aAlterations in the helicoverpa armigera midgut digestive physiology after ingestion of pigeon pea inducible leucine aminopeptidase0 aAlterations in the helicoverpa armigera midgut digestive physiol  a1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USAbPUBLIC LIBRARY SCIENCEcSEP  ae748890 v83 a<p>Jasmonate inducible plant leucine aminopeptidase (LAP) is proposed to serve as direct defense in the insect midgut. However, exact functions of inducible plant LAPs in the insect midgut remain to be estimated. In the present investigation, we report the direct defensive role of pigeon pea inducible LAP in the midgut of Helicoverpa armigera (Lepidoptera: Noctuidae) and responses of midgut soluble aminopeptidases and serine proteinases upon LAP ingestion. Larval growth and survival was significantly reduced on the diets supplemented with pigeon pea LAP. Aminopeptidase activities in larvae remain unaltered in presence or absence of inducible LAP in the diet. On the contrary, serine proteinase activities were significantly decreased in the larvae reared on pigeon pea LAP containing diet as compared to larvae fed on diet without LAP. Our data suggest that pigeon pea inducible LAP is responsible for the degradation of midgut serine proteinases upon ingestion. Reduction in the aminopeptidase activity with LpNA in the H. armigera larvae was compensated with an induction of aminopeptidase activity with ApNA. Our findings could be helpful to further dissect the roles of plant inducible LAPs in the direct plant defense against herbivory.</p>1 aLomate, Purushottam, R.1 aJadhav, Bhakti, R.1 aGiri, Ashok, P.1 aHivrale, Vandana, K.  uhttps://library.ncl.res.in/content/alterations-helicoverpa-armigera-midgut-digestive-physiology-after-ingestion-pigeon-pea-002840nas a2200241   4500008004100000022001400041245009000055210006900145260008100214300000700295490000700302520195400309653001902263653002402282653002102306653002602327653002902353100002602382700002802408700002002436700002502456856011702481       2013                        eng d  a1471-209100aCharacterization of a chemostable serine alkaline protease from Periplaneta americana0 aCharacterization of a chemostable serine alkaline protease from   a236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLANDbBIOMED CENTRAL LTDcNOV  a320 v143 a<p>Background: Proteases are important enzymes involved in numerous essential physiological processes and hold a strong potential for industrial applications. The proteolytic activity of insects' gut is endowed by many isoforms with diverse properties and specificities. Thus, insect proteases can act as a tool in industrial processes. Results: In the present study, purification and properties of a serine alkaline protease from Periplaneta americana and its potential application as an additive in various bio-formulations are reported. The enzyme was purified near to homogeneity by using acetone precipitation and Sephadex G-100 gel filtration chromatography. Enzyme activity was increased up to 4.2 fold after gel filtration chromatography. The purified enzyme appeared as single protein-band with a molecular mass of similar to 27.8 kDa in SDS-PAGE. The optimum pH and temperature for the proteolytic activity for purified protein were found around pH 8.0 and 60 degrees C respectively. Complete inhibition of the purified enzyme by phenylmethylsulfonyl fluoride confirmed that the protease was of serine-type. The purified enzyme revealed high stability and compatibility towards detergents, oxidizing, reducing, and bleaching agents. In addition, enzyme also showed stability towards organic solvents and commercial detergents. Conclusion: Several important properties of a serine protease from P. Americana were revealed. Moreover, insects can serve as excellent and alternative source of industrially important proteases with unique properties, which can be utilized as additives in detergents, stain removers and other bio-formulations. Properties of the P. americana protease accounted in the present investigation can be exploited further in various industrial processes. As an industrial prospective, identification of enzymes with varying essential properties from different insect species might be good approach and bioresource.</p>10aChemostability10aIndustrial catalyst10aInsect proteases10aPeriplaneta americana10aSerine alkaline protease1 aSanatan, Prashant, T.1 aLomate, Purushottam, R.1 aGiri, Ashok, P.1 aHivrale, Vandana, K.  uhttps://library.ncl.res.in/content/characterization-chemostable-serine-alkaline-protease-periplaneta-americana-002473nas a2200241   4500008004100000022001400041245013400055210006900189260007400258300001200332490000600344520154200350653002001892653002501912653002301937653002601960653001501986100002502001700002802026700002802054700002102082856012802103       2013                        eng d  a1872-885500aCompensatory proteolytic responses to dietary proteinase inhibitors from Albizia lebbeck seeds in the helicoverpa armigera larvae0 aCompensatory proteolytic responses to dietary proteinase inhibit  aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcJUN  a259-2660 v73 a<p>Plant proteinase inhibitors (PIs) have been shown to reduce the growth rates in larvae of numerous insect species. On the other hand, insects can also regulate their proteinases against plant PIs. In the present study, we report the compensatory activities of Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) gut proteinases against the PIs of Albizia lebbeck seeds. Total of ten proteinase inhibitor bands were detected in the seed extract of A. lebbeck. Bioassays were conducted by feeding H. armigera larvae on diet containing partially purified PIs from A. lebbeck seeds. Results show that larval growth and survival was significantly reduced by A. lebbeck PIs. We found that higher activity H. armigera gut proteinase (HGP) isoforms observed in the midgut of control larvae were inhibited in the midgut of larvae fed on test diet. Some HGP isoforms were induced in the larvae fed on PI containing test diet; however, these isoforms showed lower activity in the larvae fed on control diet. Aminopeptidase activities were significantly increased in the midgut of larvae fed on test diet. A population of susceptible and resistant enzymes was observed in the midgut of H. armigera, when fed on diet containing PIs from A. lebbeck seeds. Our initial observations indicate that H. armigera can regulate its digestive proteinase activity against non-host plant PIs, too. It is important to study the exact biochemical and molecular mechanisms underlying this phenomenon in order to develop PI-based insect control strategies.</p>10aAlbizia lebbeck10aHelicoverpa armigera10aMidgut proteinases10aProteinase inhibitors10aregulation1 aHivrale, Vandana, K.1 aLomate, Purushottam, R.1 aBasaiyye, Shriniwas, S.1 aKalve, Neeta, D.  uhttps://library.ncl.res.in/content/compensatory-proteolytic-responses-dietary-proteinase-inhibitors-albizia-lebbeck-seeds-0