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1

A kidney bean trypsin inhibitor with an insecticidal potential against Helicoverpa armigera and Spodoptera litura

100%
Mittal A., Kansal R., Kalia V., Tripathi M., Gupta V. K.
Acta Physiologiae Plantarum
|
2014
|
tom 36
|
nr 02
In the present study, trypsin inhibitor extracts of ten kidney bean seed (Phaseolus vulgaris) varieties exhibiting trypsin and gut trypsin-like protease inhibitor activity were tested on Helicoverpa armigera and Spodoptera litura. Trypsin inhibitor protein was isolated and purified using multi-step strategy with a recovery of ~15 % and purification fold by ~39.4. SDS-PAGE revealed a single band corresponding to molecular mass of ~15 kDa and inhibitory activity was confirmed by reverse zymogram analyses. The inhibitor retained its inhibitory activity over a broad range of pH (3–11), temperature (40–60°C) and thermostability was promoted by casein, CaCl₂, BSA and sucrose. The purified inhibitor inhibited bovine trypsin in 1:1 molar ratio. Kinetic studies showed that the protein is a competitive inhibitor with an equilibrium dissociation constant of 1.85 μM. The purified trypsin inhibitor protein was further incorporated in the artificial diet and fed to second instar larvae. A maximum of 91.7 % inhibition was obtained in H. armigera, while it was moderate in S. litura (29 %) with slight varietal differences. The insect bioassay showed 40 and 22 % decrease in larval growth followed by 3 and 2 days delay in pupation of H. armigera and S. litura, respectively. Some of the adults emerged were deformed and not fully formed. Trypsin inhibitor protein was more effective against H. armigera as it showed 46.7 % mortality during larval growth period compared to S. litura (13.3 %).
2

Purification, characterization and evaluation of insecticidal potential of trypsin inhibitor from mungbean (Vigna radiata L. Wilczek) seeds

100%
Kansal R., Gupta R. N., Koundal K. R., Kuhar K., Gupta V. K.
Acta Physiologiae Plantarum
|
2008
|
tom 30
|
nr 6
Protease inhibitors present in seeds of legumes possess strong inhibitory activity against trypsin and confer resistance against pests. In the present investigation, trypsin inhibitor activity was found in the seed flour extracts of all the eight selected varieties of mungbean under study which was further confirmed by dot blot analysis. All the varieties showed inhibitory activity in vitro against the gut protease of Helicoverpa armigera (HGP). Trypsin inhibitor was purified from mungbean seeds to near homogeneity with 58.1-fold and 22.8% recovery using heat denaturation, NH4(SO4)2 fractionation, ion-exchange chromatography on DEAE-Sephadex A-25 and gel filtration through Sephadex G-75. The molecular mass of the inhibitor was 47 kDa as determined by gel filtration and SDS-PAGE. The inhibitor retained 90% or more activity between pH 4 and 10, however, it was nearly inactive at extreme pH values. The inhibitor was stable up to 80℃ but thereafter, the activity decreased gradually retaining nearly 30% of activity when heated at 100℃ for 20 min. The inhibitor activity was undetectable at 121℃. Insect bioassay experiment using purified mungbean trypsin inhibitor showed a marked decline in survival (%) of larvae with increase in inhibitor concentration. The larval growth was also extended by the trypsin inhibitor. This study signifies the insecticidal potential of mungbean trypsin inhibitor which might be exploited for raising transgenic plants.
3

A Bowman–Birk protease inhibitor with antifeedant and antifungal activity from Dolichos biflorus

86%
Kuhar K., Kansal R., Subrahmanyam B., Koundal K. R., Miglani K., Gupta V. K.
Acta Physiologiae Plantarum
|
2013
|
tom 35
|
nr 06
In the present study, 11 varieties of Dolichos biflorus exhibited both protease inhibitor activities as well as in vitro inhibitory activity against Helicoverpa armigera gut protease. A Bowman–Birk protease inhibitor showing activity against trypsin and α-chymotrypsin has been purified from D. biflorus seeds using multi-step strategy. The purified inhibitor revealed a single band on SDSPAGE corresponding to molecular mass of 16 kDa. The inhibitory constants for the interaction of purified PI with trypsin and α-chymotrypsin were 0.04 and 0.48 lM, respectively. The purified inhibitor was stable over a pH range of 2–12 and up to a temperature of 100 ºC for 20 min. The results of insect bioassay against H. armigera revealed 68 % decline in larval weight after 7 days of feeding on artificial diet containing the inhibitor. The larval growth and % leaf area eaten were drastically reduced in the presence of inhibitor. The observed cumulative mortality from larval to adult was 51.21 %. The inhibitor displayed antifungal activity against Alternaria alternata, Fusarium oxysporum, and Aspergillus niger with minimum inhibitory concentration as 0.4, 0.6, and 1.2 μg mL-1, respectively. This is the first report of anti-feedant and anti-fungal activities of D. biflorus protease inhibitor on a single protein, which might be important for developing transgenic plants resistant to insect pests and fungal pathogens.
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