4.5 Article

Characterization and insecticidal properties of globulins and albumins from Luetzelburgia auriculata (Allemao) Ducke seeds towards Callosobruchus maculatus (F.) (Coleoptera : Bruchidae)

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JOURNAL OF STORED PRODUCTS RESEARCH
卷 43, 期 4, 页码 459-467

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PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jspr.2006.12.007

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Callosobruchus maculatus; legume; Luetzelburgia auriculata; lectin; protein; proteases

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We evaluated the development of Callosobruchus maculatus growing in artificial seeds composed of Vigna unguiculata (cowpea) seed flour mixed with exogenous proteins from Luetzelburgia auriculata. Albumin and globulin fractions from Luetzelburgia auriculata were characterized in terms of protein content, amino acid composition and antimetabolic proteins (trypsin/chymotrypsin inhibitory, porcine pancreatic alpha-amylase inhibitory, lectin activity and presence of chitin-binding proteins). Both fractions were distinct in terms of protein content and diversity as determined by electrophoresis. Lectin activity was present only in the globulins. Neither fraction exhibited inhibitory activity towards porcine pancreatic alpha-amylase but trypsin inhibition was observed. Interestingly, chitin-binding proteins were detected in both protein classes. Albumins had a severe effect upon larval development and were detrimental to insect emergence (LD50 = 0.4%) while globulins displayed slight toxicity upon larval development and no effect towards insect emergence. The presence of serine proteinase inhibitory activity and chitin binding proteins could explain, at least in part, the harmful effects on C maculatus development while lectin activity and amino acid availability seem not to correlate with any deleterious effects. Luetzelburgia auriculata would be an interesting source of seed proteins to study behavior of C maculatus upon infestation and genes coding for insecticidal proteins could become candidates for molecular biology programs devoted to producing transgenic seeds expressing resistance towards the beetle. (c) 2007 Elsevier Ltd. All rights reserved.

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