Purificação e caracterização de um inibidor de tripsina de sementes de Phaseolus vulgaris L. cultivar IAC carioca

Autores

  • Luzia Aparecida Pando Universidade Estadual do Sudoeste da Bahia
  • Silvana Cristina Pando Universidade Federal de Mato Grosso do Sul

DOI:

https://doi.org/10.22481/exon.v8i1.20438

Palavras-chave:

PvTI, Bowman-Birk, Fusarium

Resumo

Inibidores de proteinases são proteínas ou peptídeos capazes de interagir específica e reversivelmente com enzimas proteolíticas e são amplamente distribuídos no reino vegetal. Este trabalho teve como objetivos purificar e caracterizar um inibidor de tripsina de sementes de Phaseolus vulgaris L. cultivar IAC carioca por cromatografia de troca iônica em DEAE Sepharose e cromatografia líquida de alta performance (HPLC). O inibidor, nomeado PvTI, exibiu uma massa molecular aparente de 14 kDa em eletroforese em gel de poliacrilamida (SDS-PAGE) e foi capaz de inibir tripsina bovina, mas não quimotripsina. O valor da constante de inibição (Ki) contra tripsina bovina foi 3,7 x 10-8 M. A sequência N-terminal do PvTI, GDDVKSA-CCDTCLCTKSEPPTCRCVDV, apresentou alta homologia com outros inibidores tipo Bowman-Birk. PvTI exerceu efeito fungistático sobre Fusarium moniliforme na concentração de 500 μg/mL.

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Publicado

2017-06-29

Como Citar

PANDO, Luzia Aparecida; PANDO, Silvana Cristina. Purificação e caracterização de um inibidor de tripsina de sementes de Phaseolus vulgaris L. cultivar IAC carioca. Exatas Online, [S. l.], v. 8, n. 1, p. 1–12, 2017. DOI: 10.22481/exon.v8i1.20438. Disponível em: https://periodicos2.uesb.br/exon/article/view/20438. Acesso em: 2 out. 2026.