Artículos de revistas
Biochemical Aspects of a Serine Protease from Caesalpinia echinata Lam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins
Fecha
2012Registro en:
SCIENTIFIC WORLD JOURNAL, NEW YORK, v. 34, n. 1, supl. 1, Part 6, pp. 108-113, FEB 28, 2012
1537-744X
10.1100/2012/562715
Autor
Praxedes-Garcia, Priscila
Cruz-Silva, Ilana
Gozzo, Andrezza Justino
Nunes, Viviane Abreu
Torquato, Ricardo Jose
Tanaka, Aparecida Sadae
Figueiredo-Ribeiro, Rita de Cassia
Gonzalez Gonzalez, Yamile
Araujo, Mariana da Silva
Institución
Resumen
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.