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

By Priscila Praxedes-Garcia, Ilana Cruz-Silva, Andrezza Justino Gozzo, Viviane Abreu Nunes, Ricardo José Torquato, Aparecida Sadae Tanaka, Rita de Cássia Figueiredo-Ribeiro, Yamile Gonzalez Gonzalez and Mariana da Silva Araújo

Abstract

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 (Km 55.7 μM) in an optimum pH of 7.1, and this activity is effectively retained until 50°C. CeSP remained stable in the presence of kosmotropic anions (PO4 3−, SO4 2−, 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

Topics: Research Article
Publisher: The Scientific World Journal
OAI identifier: oai:pubmedcentral.nih.gov:3354420
Provided by: PubMed Central
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