Purification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreus

Autor(es)

Biaggio, Rafael Tage ^[1] ; da Silva, Ronivaldo Rodrigues ^[2] ; da Rosa, Nathalia Gonsales ^[1] ; Ribeiro Leite, Rodrigo Simoes ^[3] ; Arantes, Eliane Candiani ^[4] ; de Freitas Cabral, Tatiana Pereira ^[5] ; Juliano, Maria A. ^[6] ; Juliano, Luiz ^[6] ; Cabral, Hamilton ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Pharmaceut Sci, S-N Cafe, BR-14040903 Ribeirao Preto - Brazil

^[2] Univ Estadual Paulista, Inst Biosci Letters & Exact Sci, Sao Jose Do Rio Preto - Brazil

^[3] Fed Univ Grande Dourados, Fac Biol & Environm Sci, Dourados - Brazil

^[4] Univ Sao Paulo, Fac Pharmaceut Sci Ribeirao Preto, Dept Chem & Phys, BR-14040903 Ribeirao Preto - Brazil

^[5] Univ Ctr Educ Fdn Barretos, Fac Pharm, Barretos - Brazil

^[6] Univ Fed Sao Paulo, Paulista Sch Med, Dept Biophys, Sao Paulo - Brazil

• Tipo de documento: Artigo Científico
• Fonte: PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY; v. 46, n. 3, p. 298-304, 2016.
• Citações Web of Science: 8

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. (AU)

• Processo FAPESP: 11/06986-0 - Determinação da especificidade de peptidases isoladas de fungos usando peptídeos FRET como substratos
• Beneficiário: Hamilton Cabral
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 12/24703-8 - Análises proteômicas de fungos filamentosos meso e termofílicos expostos aos fatores físico e químico
• Beneficiário: Hamilton Cabral
• Modalidade de apoio: Auxílio à Pesquisa - Regular