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

Autor(es)

Souza, Paula Monteiro ; Werneck, Gabriela ; Aliakbarian, Bahar ; Siqueira, Felix ; Ferreira Filho, Edivaldo Ximenes ; Perego, Patrizia ; Converti, Attilio ; Magalhaes, Perola Oliveira ; Pessoa Junior, Adalberto

• Tipo de documento: Artigo Científico
• Fonte: Food and Chemical Toxicology; v. 109, p. 8-pg., 2017-11-01.

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
• Modalidade de apoio: Bolsas no Brasil - Doutorado