Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins

• Autor(a) principal: Praxedes-Garcia, Priscila [UNIFESP]
• Data de Publicação: 2012
• Outros Autores: Cruz-Silva, Ilana [UNIFESP], Gozzo, Andrezza Justino [UNIFESP], Nunes, Viviane Abreu, Torquato, Ricardo Jose [UNIFESP], Tanaka, Aparecida Sadae [UNIFESP], Figueiredo-Ribeiro, Rita de Cassia, Gonzalez Gonzalez, Yamile, Araujo, Mariana da Silva [UNIFESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNIFESP
• Texto Completo: http://repositorio.unifesp.br/handle/11600/34350; http://dx.doi.org/10.1100/2012/562715

Several proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds of Caesalpinia echinata Lam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatographies and gel filtration. This 61-kDa serine protease (CeSP) hydrolyses H-D-prolyl-L-phenylalanyl-L-arginine-p-nitroanilide (K-m 55.7 mu M) in an optimum pH of 7.1, and this activity is effectively retained until 50 degrees C. CeSP remained stable in the presence of kosmotropic anions (PO43-, SO42-, and CH3COO-) or chaotropic cations (K+ and Na+). It is strongly inhibited by TLCK, a serine protease inhibitor, but not by E-64, EDTA or pepstatin A. the characteristics of the purified enzyme allowed us to classify it as a serine protease. the role of CeSP in the seeds cannot be assigned yet but is possible to infer that it is involved in the mobilization of seed storage proteins.