Purification and biochemical characterization of an extracellular serine peptidase from aspergillus terreus
Data
2016
Tipo
Artigo
Título da Revista
ISSN da Revista
Título de Volume
Resumo
Peptidases are important because they play a central role in pharmaceutical, food, environmental, and other industrial processes. A serine peptidase from Aspergillus terreus was isolated after two chromatography steps that showed a yield of 15.5%. Its molecular mass was determined to be 43 kD, by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). This peptidase was active between pH 5.0 to 8.0 and had maximum activity at pH 7.0, at 45 degrees C. When exposited with 1 M of urea, the enzyme maintained 100% activity and used azocasein as substrate. The N-terminal (first 15 residues) showed 33% identity with the serine peptidase of Aspergillus clavatus ES1. The kinetics assays showed that subsite S-2 did not bind polar basic amino acids (His and Arg) nonpolar acidic amino acids (Asp and Glu). The subsite S-1 showed higher catalytic efficiency than the S-2 and S-3 subsites.
Descrição
Citação
Preparative Biochemistry & Biotechnology. Philadelphia, v. 46, n. 3, p. 298-304, 2016.