Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/244350
Type: Artigo
Title: Purification and characterization of a Kunitz inhibitor from Poincianella pyramidalis with insecticide activity against the Mediterranean flour moth
Author: Guimarães, Lays Cordeiro
Oliveira, Caio Fernando Ramalho de
Marangoni, Sergio
Oliveira, Daniella Gorete Lourenço de
Macedo, Maria Lígia Rodrigues
Abstract: This paper describes the characterization of a trypsin inhibitor from Poincianella pyramidalis seeds (PpyTI). The partial sequencing of PpyTI revealed homology to Kunitz inhibitors, clustered as a member of Family 103 in MEROPS database. PpyTI has a single polypeptide chain of 19,042 Da and presents stability at high temperatures (up to 70 degrees C) and a wide range of pH. In vitro assays showed that disulfide bridges have an important stabilization role of reactive site in PpyTI, a characteristic shared among several Kunitz inhibitors. Bioassays carried out with the Mediterranean flour moth (Anagasta kuehniella) revealed a significant decrease in both larval weight and survival of PpyTI-fed larvae, besides a larval stage extension. Through biochemical analysis, we demonstrated that the PpyTI insecticide effects were triggered by digestion process commitment, through the inhibition of trypsin and chymotrypsin activities, the major digestive enzymes in this species. The insecticide effects and biochemical characterization of PpyTI encourage further studies using this inhibitor for insect pest control. (C) 2014 Elsevier Inc. All rights reserved.
This paper describes the characterization of a trypsin inhibitor from Poincianella pyramidalis seeds (PpyTI). The partial sequencing of PpyTI revealed homology to Kunitz inhibitors, clustered as a member of Family 103 in MEROPS database. PpyTI has a single polypeptide chain of 19,042 Da and presents stability at high temperatures (up to 70 degrees C) and a wide range of pH. In vitro assays showed that disulfide bridges have an important stabilization role of reactive site in PpyTI, a characteristic shared among several Kunitz inhibitors. Bioassays carried out with the Mediterranean flour moth (Anagasta kuehniella) revealed a significant decrease in both larval weight and survival of PpyTI-fed larvae, besides a larval stage extension. Through biochemical analysis, we demonstrated that the PpyTI insecticide effects were triggered by digestion process commitment, through the inhibition of trypsin and chymotrypsin activities, the major digestive enzymes in this species. The insecticide effects and biochemical characterization of PpyTI encourage further studies using this inhibitor for insect pest control
Subject: Fabaceae
Inibidores da tripsina
Anagasta kuehniella
Inseto - Controle
Inseticidas
Country: Estados Unidos
Editor: Elsevier
Citation: Purification And Characterization Of A Kunitz Inhibitor From Poincianella Pyramidalis With Insecticide Activity Against The Mediterranean Flour Moth. Academic Press Inc Elsevier Science, v. 118, p. 1-9 FEB-2015.
Rights: fechado
Identifier DOI: 10.1016/j.pestbp.2014.12.001
Address: http://www.sciencedirect.com/science/article/pii/S0048357514002284
Date Issue: 2015
Appears in Collections:IB - Artigos e Outros Documentos

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