Purification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreus
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Data
2016-01-01
Autores
Biaggio, Rafael Tage
Silva, Ronivaldo Rodrigues da [UNESP]
Rosa, Nathalia Gonsales da
Ribeiro Leite, Rodrigo Simoes
Arantes, Eliane Candiani
Freitas Cabral, Tatiana Pereira de
Juliano, Maria A.
Juliano, Luiz
Cabral, Hamilton
Título da Revista
ISSN da Revista
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Editor
Taylor & Francis Inc
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
Palavras-chave
Aspergillus, enzyme kinetics, filamentous fungi, N-terminal sequence, protease, protein
Como citar
Preparative Biochemistry & Biotechnology. Philadelphia: Taylor & Francis Inc, v. 46, n. 3, p. 298-304, 2016.