A Trypsin Inhibitor from Sapindus saponaria L. Seeds: Purification,Characterization, and Activity Towards Pest Insect Digestive Enzyme |
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| Authors: | Maria Lígia R. Macedo Eduardo B. S. Diz Filho Mariadas Graças M. Freire Maria Luiza V. Oliva Joana T. Sumikawa Marcos H. Toyama Sérgio Marangoni |
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| Affiliation: | 1.Laboratório de Purifica??o de Proteínas e suas Fun??es Biológicas, Departamento de Tecnologia de Alimentos e Saúde Pública, Centro de Ciências Biológicas e da Saúde,Universidade Federal do Mato Grosso do Sul (UFMS),Campo Grande,Brazil;2.Departamento de Bioquímica,Instituto de Biologia,Campinas,Brazil;3.Laboratório de Química e Biomoléculas, Centro de Pesquisa,Institutos Superiores do CENSA,Campos dos Goytacazes,Brazil;4.Departamento de Bioquímica,Escola Paulista de Medicina, UNIFESP,S?o Paulo,Brazil |
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| Abstract: | The present paper describes the purification, characterization and determination of the partial primary structure of the first trypsin inhibitor isolated from the family Sapindaceae. A highly stable, potent trypsin inhibitor (SSTI) was purified to homogeneity. SDS–PAGE analysis revealed that the protein consists of a two-polypeptide chain with molecular masses of approximately 15 and 3 kDa. The purified inhibitor inhibited bovine trypsin at a 1:1 M ratio. Kinetic analysis revealed that the protein is a competitive inhibitor with an equilibrium dissociation constant of 10−9 M for trypsin. The partial NH2- terminal sequence of 36 amino acids in SSTI indicates homology with other members of the trypsin-inhibitor family from different sources. This inhibitor is highly stable in the presence of denaturing agents. SSTI showed significant inhibitory activity against trypsin-like proteases present in the larval midgut on Anagasta kuehniella, Corcyra cephalonica, Diatreae saccharalis and Anticarsia gemmatalis. |
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