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|Type:||Artigo de periódico|
|Title:||Purification of a Kunitz-type Inhibitor from Acacia polyphylla DC Seeds: Characterization and Insecticidal Properties against Anagasta kuehniella Zeller (Lepidoptera: Pyralidae)|
de Oliveira, CFR
|Abstract:||Anagasta kuehniella is a polyphagous pest that causes economic losses worldwide. This species produces serine proteases as its major enzymes for protein digestion. In this study, a new serine-protease inhibitor was isolated from Acacia polyphylla seeds (AcKI). Further analysis revealed that AcKI is formed by two polypeptide chains with a relative molecular mass of similar to 20 kDa. The effects of AcKI on the development, survival, and enzymatic activity of Anagasta kuehniella larvae were evaluated, by incorporating AcKI in an artificial diet Bioassays revealed a reduction in larval weight of similar to 50% with the lower concentration of AcKI used in the study (0.5%). Although additional assays 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.|
|Editor:||Amer Chemical Soc|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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