Molecular Identification of Four Different α-amylase Inhibitors from Baru (Dipteryx alata) Seeds with Activity Toward Insect Enzymes
| Autor: | Raul Alberto Laumann, Carlos J. Bloch, Octavio L. Franco, Eliane Ferreira Noronha, Betania Ferraz Quirino, Maria Fatima Grossi-de-Sa, Patrícia B. Pelegrini, Krishna B. Bonavides, Jorge Alex Taquita Melo |
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| Rok vydání: | 2007 |
| Předmět: |
Insecta
Biochemistry Chromatography Affinity α-amylase inhibitors Botany Animals Bioassay Enzyme Inhibitors Molecular Biology Dipteryx biology Plant Extracts Bean weevil Dipteryx alata Weevil Callosobruchus maculates food and beverages General Medicine biology.organism_classification Molecular Weight Callosobruchus maculatus Horticulture Anthonomus Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Seeds biology.protein Biological Assay Electrophoresis Polyacrylamide Gel PEST analysis alpha-Amylases Digestion Alpha-amylase |
| Zdroj: | Repositório Institucional da UCB Universidade Católica de Brasília (UCB) instacron:UCB |
| ISSN: | 1976-6696 |
| DOI: | 10.5483/bmbrep.2007.40.4.494 |
| Popis: | Made available in DSpace on 2016-10-10T03:52:58Z (GMT). No. of bitstreams: 5 Molecular Identification of Four Different.PDF: 1077082 bytes, checksum: f6590fcfbf1bfa8d892b75a77f30e5d5 (MD5) license_url: 52 bytes, checksum: 2f32edb9c19a57e928372a33fd08dba5 (MD5) license_text: 24372 bytes, checksum: 94b0a37ff5ec51de8c55507bff4a7ff9 (MD5) license_rdf: 24623 bytes, checksum: 378d22d8fe50e084ee2f354be78cbe62 (MD5) license.txt: 1887 bytes, checksum: 445d1980f282ec865917de35a4c622f6 (MD5) Previous issue date: 2007-07 The endophytic bruchid pest Callosobruchus maculatus causes severe damage to storage cowpea seeds, leading to economical losses. For this reason the use of α-amylase inhibitors to interfere with the pest digestion process has been an interesting alternative to control bruchids. With this aim, α-amylase inhibitors from baru seeds (Dipteryx alata) were isolated by affinity chromatographic procedures, causing enhanced inhibition of C. maculatus and Anthonomus grandis α-amylases. To attempt further purification, this fraction was applied onto a reversed-phase HPLC column, generating four peaks with remarkable inhibition toward C. maculatus α-amylases. SDS-PAGE and MALDI-ToF analysis identified major proteins of approximately 5.0, 11.0, 20.0 and 55 kDa that showed α-amylase inhibition. Results of in vivo bioassays using artificial seeds containing 1.0% (w/w) of baru crude extract revealed 40% cowpea weevil larvae mortality. These results provide evidence that several α-amylase inhibitors classes, with biotechnological potential, can be isolated from a single plant species. Sim Publicado |
| Databáze: | OpenAIRE |
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