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Vicilin from Anadenanthera colubrina Seeds: An alternative tool to combat Callosobruchus maculatus.
França, A F J; Araújo, J N; Santos, Y Q; Carelli, G S C; Silva, D A; Amorim, T M L; Migliolo, L; Santos, E A; Oliveira, A S; Uchôa, A F.
Affiliation
  • França AFJ; Laboratório de Química e Função de Proteínas Bioativas - LQFPB, Departamento de Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil.
  • Araújo JN; Escola Multicampi de Ciências Médicas - EMCM, Universidade Federal do Rio Grande do Norte, Caicó, RN, Brazil.
  • Santos YQ; Laboratório de Química e Função de Proteínas Bioativas - LQFPB, Departamento de Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil.
  • Carelli GSC; Laboratório de Química e Função de Proteínas Bioativas - LQFPB, Departamento de Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil.
  • Silva DA; Instituto Federal do Ceará, Campus Limoeiro do Norte, Limoeiro do Norte, CE, Brazil.
  • Amorim TML; Laboratório de Química e Função de Proteínas Bioativas - LQFPB, Departamento de Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil.
  • Migliolo L; Laboratório de Produtos Naturais - LPN, Centro de Ciências da Saúde e Desporto, Universidade Federal do Acre, Rio Branco, AC, Brazil.
  • Santos EA; Curso de Bacharelado em Medicina - Núcleo de Pesquisa em Ciências Médicas/NPCMed, Universidade Federal do Piauí, Picos, PI, Brazil.
  • Oliveira AS; Laboratório de Química e Função de Proteínas Bioativas - LQFPB, Departamento de Bioquímica, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil.
  • Uchôa AF; Laboratório S-Inova Biotech, Pós-Graduação em Biotecnologia, Universidade Católica Dom Bosco, Brazil.
Saudi J Biol Sci ; 28(9): 5229-5237, 2021 Sep.
Article in En | MEDLINE | ID: mdl-34466101
ABSTRACT
Vicilins are seed proteins, and they constitute 70-80% of the total protein in leguminous seeds; with amolecular mass between 150 and 190 kDa, they are composed of subunits without disulfide bridges, with high affinity for chitin-binding. They are also associated with seed defense against insect pests. The chitin-binding vicilin from Anadenanthera colubrina seeds was purified by ammonium sulfate, followed by affinity chromatography on a chitin column, molecular exclusion on Superdex 75 Tricorn in FPLC system and Phenomenex C8 chromatography in HPLC system. The A. colubrina vicilin, named AcV, is a tetrameric glycoprotein composed of 1.55% carbohydrates and molecular weight determined by SDS-PAGE, consisting of 70, 73, 43 and 41 kDa. The AcV homogeneity was confirmed in native PAGE, where it was observed to be a unique band with slow mobility in this gel, with approximately 230 kDa. AcV added to the Callosobruchus maculatus diet in the bioassays resulted in a strong effect on adult emergence (ED50 of 0.096%), and in larvae caused a marked reduction in mass (WD50 of 0.32%) and lethality (LD50 of 0.33%) (ww). The digestibility of AcV was evaluated in vitro with the digestive enzymes of larvae of C. maculatus of fourth instar, showing major fragments of 10 and 30 kDa. AcV showed reactivity against the anti-EvV antibody from Erythrina velutina vicilin. The deleterious effects of AcV are likely to be associated with the chitin-binding fragments generated by proteolysis in the bruchid gut, similarly to that found for vicilins from other leguminous plant species, Enterolobium contortisiliquum and Vigna unguiculata. AcV might be a candidate protein for a possible bioinsecticidal control of the bruchid weevil, C. maculatus.
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Saudi J Biol Sci Year: 2021 Type: Article Affiliation country: Brazil

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Saudi J Biol Sci Year: 2021 Type: Article Affiliation country: Brazil