Purification and Characterisation of a 31-kDa Chitinase from the Myzus Persicae Aphid: A Target for Hemiptera Biocontrol
| Autor: | Charles Vincent, Philippe Giordanengo, Sophie Vandermoten, Eric Haubruge, Frédéric Francis, Anas Cherqui, Edwin De Pauw, Julien Saguez, Marie-France Versali, Jacques Dommes |
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| Rok vydání: | 2012 |
| Předmět: |
Bioengineering
Peptide Fractionation Biology Applied Microbiology and Biotechnology Biochemistry Acetylglucosamine chemistry.chemical_compound Animals Ammonium Disulfides Enzyme Inhibitors Pest Control Biological Molecular Biology chemistry.chemical_classification Aphid Chitinases General Medicine biology.organism_classification Molecular Weight Enzyme chemistry Concanavalin A Aphids Chitinase biology.protein Tyrosine Myzus persicae Trisaccharides Biotechnology |
| Zdroj: | Applied Biochemistry and Biotechnology. 166:1291-1300 |
| ISSN: | 1559-0291 0273-2289 |
| DOI: | 10.1007/s12010-011-9517-3 |
| Popis: | Hydrolytic enzymes involved in chitin degradation are important to allow moulting during insect development. Chitinases are interesting targets to disturb growth and develop alternative strategies to control insect pests. In this work, a chitinase from the aphid Myzus persicae was purified with a 36-fold purification rate in a three step procedure by ammonium sulphate fractionation, anion-exchange chromatography on a DEAE column and on an affinity Concanavalin A column. The purified chitinase purity assessed by 1D and 2D SDS-PAGE revealed a single band and three spots at 31 kDa, respectively. Chitinases were found to have high homologies with Concanavalins A and B, two chitinase-related proteins, a fungal endochitinase and an aphid acetylhydrolase by peptide identification by Maldi-Tof-Tof. The efficiency of two potent chitinase inhibitors, namely allosamidin and psammaplin A, was tested and showed significant rate of enzymatic inhibition. |
| Databáze: | OpenAIRE |
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