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Studies on selected protease and amylase inhibitors of helicoverpa armigera

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Title Studies on selected protease and amylase inhibitors of helicoverpa armigera
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Contributor Kamble L. H.
 
Subject —
 
Description Helicoverpa armigera (Hübner) is a lepidopteran pest destruct many important
newlinecrop plants. Use of chemical insecticide to control H. armigera failed due to
newlinedevelopment of resistance in insect, environmental and health hazards. Development
newlineof transgenic plants using genes of protease inhibitors, and amylase inhibitors of plant
newlineorigin is an approach which needs to be exploited for development of insect resistant
newlineplants. All host plants of Helicoverpa posses digestive enzyme inhibitors as a tool for
newlinedefense against Helicoverpa.
newlineIn present study host plant parts of Lablab purpureus have been screened for
newlinepresence of trypsin inhibitors (LPTI), chymotrypsin inhibitors (LPCI) and amylase
newlineinhibitors (LPAI) of Helicoverpa armigera using spectrophotometric assay method
newlineand electrophoretic analysis. Lablab purpureus is a crop plant belonging to the family
newlineLeguuminosae. A proteinacious inhibitor of trypsin and chymotrypsin was isolated
newlinefrom Lablab purpureus seeds. Protein was extracted in 0.1 M tris Cl buffer (pH-8.0)
newlineand subject to precipitation using 20% ammonium sulphate, dialyzed against 0.02 M
newlinephosphate buffer and the dialyzed Lablab purpureus protease inhibitors (LPPI) eluted
newlineon DEAE cellulose column and affinity column. Fold purification obtained in final
newlinestep of purification was 13.0 of LPTI and 12.88 of LPCI. Purified sample was
newlineanalyzed on gelatin embedded native PAGE for isoform detectetion. Three isoforms
newlineof LPTI were observed on SDS-PAGE after ion exchange column. SDS-PAGE
newlineanalysis of Lablab purpures protease inhibitor (LPPI) showed two bands of molecular
newlineweight ~21.17 kDa and 20.33 kDa after affinity chromatography. Solution assay
newlineshowed 24 and#61549;g of inhibitor concentration causes 50% inhibition of LPTI and 28 and#61549;g of
newlineLPCI. Thermo stability study showed that the LPPI are quite thermostable. It lost
newlineAbstract
newlineII
newlinecomplete activity when heated at 100and#61616;C for 70 minute. LPPI showed activity against
newlineH. armigera protease between pH ranges 6.0 to 8.0.
newlineA proteinacious inhibitor of amylase (LPAI) was isolated
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Date 2017-06-08T09:16:35Z
2017-06-08T09:16:35Z
22/03/2011
29/03/2016
11/02/2017
 
Type Ph.D.
 
Identifier http://hdl.handle.net/10603/153259
 
Language English
 
Relation 156b
 
Rights university
 
Format 124p
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None
 
Coverage Biotechnology
 
Publisher Nanded
Swami Ramanand Teerth Marathwada University
School of Life Sciences
 
Source University