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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Production, purification and characterization of an aspartic protease from Aspergillus foetidus

Texto completo
Autor(es):
Souza, Paula Monteiro [1, 2] ; Werneck, Gabriela [2] ; Aliakbarian, Bahar [3] ; Siqueira, Felix [4] ; Ferreira Filho, Edivaldo Ximenes [5] ; Perego, Patrizia [3] ; Converti, Attilio [3] ; Magalhaes, Perola Oliveira [2] ; Pessoa Junior, Adalberto [1]
Número total de Autores: 9
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Dept Biochem & Pharmaceut Technol, Sao Paulo - Brazil
[2] Univ Brasilia, Hlth Sci Sch, Dept Pharm, Brasilia, DF - Brazil
[3] Genoa Univ, Dept Civil Chem & Environm Engn, Pole Chem Engn, Genoa - Italy
[4] Agroenergy Embrapa, Lab Biochem Proc, Brasilia, DF - Brazil
[5] Univ Brasilia, Dept Cellular Biol, Lab Enzymol, Brasilia, DF - Brazil
Número total de Afiliações: 5
Tipo de documento: Artigo Científico
Fonte: Food and Chemical Toxicology; v. 109, n. 2, p. 1103-1110, NOV 2017.
Citações Web of Science: 17
Resumo

An acidic thermostable protease was extracellularly produced either in shake flask or in stirred tank bioreactor by an Aspergillus foetidus strain isolated from the Brazilian savanna soil using different nitrogen sources. Its maximum activity (63.7 U mL(-1)) was obtained in a medium containing 2% (w/v) peptone. A cultivation carried out in a 5.0 L stirred -tank bioreactor provided a maximum protease activity 9% lower than that observed in Erlenmeyer flasks, which was obtained after a significantly shorter (by 16-29%) time. Protease purification by a combination of gel -filtration chromatography resulted in a 16.9 -fold increase in specific activity (248.1 U g(-1)). The estimated molecular weight of the purified enzyme was 50.6 kDa, and the optimal pH and temperature were 5.0 and 55 degrees C, respectively. The enzyme was completely inhibited by pepstatin A, and its activity enhanced by some metals. According to the inhibition profiles, it was confirmed that the purified acid protease belongs to the aspartic protease type. These results are quite promising for future development of large-scale production of such protease, which can be useful in biotechnological applications requiring high enzyme activity and stability under acidic conditions. (C) 2017 Elsevier Ltd. All rights reserved. (AU)

Processo FAPESP: 11/03982-3 - Produção de proteases por fungos filamentosos isolados do cerrado do centro-oeste brasileiro
Beneficiário:Paula Monteiro de Souza
Linha de fomento: Bolsas no Brasil - Doutorado