Bioinsecticidal activity of Archidendron ellipticum trypsin inhibitor on growth and serine digestive enzymes during larval development of Spodoptera litura.

  title={Bioinsecticidal activity of Archidendron ellipticum trypsin inhibitor on growth and serine digestive enzymes during larval development of Spodoptera litura.},
  author={Arindam Bhattacharyya and Sudeshna Mazumdar Leighton and Cherukuri R. Babu},
  journal={Comparative biochemistry and physiology. Toxicology \& pharmacology : CBP},
  volume={145 4},

Two Kunitz-type inhibitors with activity against trypsin and papain from Pithecellobium dumosum seeds: purification, characterization, and activity towards pest insect digestive enzyme.

Results show that both inhibitors are members of the Kunitz-inhibitor family and that they affect the digestive enzyme larvae of diverse orders, indicating a potential insect antifeedant.

Molecular cloning and insecticidal effect of Inga laurina trypsin inhibitor on Diatraea saccharalis and Heliothis virescens.

Trypsin inhibitor from Leucaena leucocephala seeds delays and disrupts the development of Aedes aegypti, a multiple-disease vector.

LTI is a promising new tool to control critical points of Ae.

Inhibitory Effect of Protease Inhibitors on Larval Midgut Protease Activities and the Performance of Plutella xylostella (Lepidoptera: Plutellidae)

Results showed that protease inhibitors had a certain extent inhibition to protease activities in the larval midgut of P. xylostella and that STI can potentially be used for effective pest control.

Dual Insecticidal Effects of Adenanthera pavonina Kunitz-Type Inhibitor on Plodia interpunctella is Mediated by Digestive Enzymes Inhibition and Chitin-Binding Properties

Investigation of the insecticidal properties of ApKTI, a Kunitz trypsin inhibitor from Adenanthera pavonina seeds, against P. interpunctella larvae showed reduction of up to 88% on larval weight and 75% in survival, suggesting a dual and promiscuous mechanisms biding to two completely different targets.

Purification of a Kunitz-type inhibitor from Acacia polyphyllaDC seeds: characterization and insecticidal properties against Anagasta kuehniella Zeller (Lepidoptera: Pyralidae).

Although additionalassays showed an increase in endogenous trypsin and chymotrypsin activities, with a degree of AcKI-insensivity, AcKI produces an anti nutritional effect on A. kuehniella, indicating AcKI as a promising bioinsecticide protein for engineering plants that are resistant to insect pests.

Bioinsecticidal activity of Murraya koenigii miraculin-like protein against Helicoverpa armigera and Spodoptera litura.

The efficacy of MKMLP is demonstrated as a potential plant defense agent against H. armigera and S. litura pests in a dose-dependent manner.

Evaluation and characterization of trypsin inhibitor from rice bean with inhibitory activity against gut proteases of Spodoptera litura

The role of rice bean protease inhibitors as a potential strategy against insectpests of economic importance is clarified and the highest TI content in the seeds nearing maturity correlates to the role of TIs in protecting against insect pests.

Inhibitors from Pigeonpea Active Against Lepidopteran Gut Proteinases

The results suggest that the inhibitory potential of PIs from pigeonpea cultivars and wild types could be exploited in management of nonhost insects.



Overproduction of Digestive Enzymes Compensates for Inhibitory Effects of Protease and α-Amylase Inhibitors Fed to Three Species of Leafrollers (Lepidoptera: Tortricidae)

In larvae chronically fed POTI or BPTI, in vitro tests showed that the sensitivity of caseinase and chymotrypsin to protease inhibitors was unchanged, and a very small amount of insensitive trypsin was produced.

In vivo bioinsecticidal activity toward Ceratitis capitata (fruit fly) and Callosobruchus maculatus (cowpea weevil) and in vitro bioinsecticidal activity toward different orders of insect pests of a trypsin inhibitor purified from tamarind tree (Tamarindus indica) seeds.

In vitro bioinsecticidal activity against insect digestive enzymes from different orders showed that TTI had remarkable activity against enzymes from coleopteran, Anthonomus grandis, Zabrotes subfasciatus, Callosobruchus maculatus, and lepidopteron.