dc.creatorMachado, SW
dc.creatorde Oliveira, CFR
dc.creatorBezerra, CDS
dc.creatorFreire, MDM
dc.creatorKill, MR
dc.creatorMachado, OLT
dc.creatorMarangoni, S
dc.creatorMacedo, MLR
dc.date2013
dc.date41334
dc.date2014-07-30T14:18:43Z
dc.date2015-11-26T16:58:51Z
dc.date2014-07-30T14:18:43Z
dc.date2015-11-26T16:58:51Z
dc.date.accessioned2018-03-28T23:46:29Z
dc.date.available2018-03-28T23:46:29Z
dc.identifierJournal Of Agricultural And Food Chemistry. Amer Chemical Soc, v. 61, n. 10, n. 2469, n. 2478, 2013.
dc.identifier0021-8561
dc.identifierWOS:000316243900022
dc.identifier10.1021/jf3049565
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/58472
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/58472
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1278039
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionAnagasta 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.
dc.description61
dc.description10
dc.description2469
dc.description2478
dc.descriptionFINEP
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFUNDECT
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageen
dc.publisherAmer Chemical Soc
dc.publisherWashington
dc.publisherEUA
dc.relationJournal Of Agricultural And Food Chemistry
dc.relationJ. Agric. Food Chem.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectAcacia polyphylla
dc.subjectKunitz-type inhibitor
dc.subjectAnagasta kuehniella
dc.subjectpest insect
dc.subjectSerine Proteinase-inhibitors
dc.subjectTrypsin-inhibitor
dc.subjectLarval Development
dc.subjectDigestive Enzymes
dc.subjectBioinsecticidal Activity
dc.subjectHubner Lepidoptera
dc.subjectHelicoverpa-zea
dc.subjectChymotrypsin
dc.subjectMidgut
dc.subjectGrowth
dc.titlePurification of a Kunitz-type Inhibitor from Acacia polyphylla DC Seeds: Characterization and Insecticidal Properties against Anagasta kuehniella Zeller (Lepidoptera: Pyralidae)
dc.typeArtículos de revistas


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