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Hernández-Martínez, R., Gutiérrez-Sánchez, G., Bergmann, C.W., Loera-Corral, O., Rojo-Domínguez, A., Huerta-Ochoa, S., Regalado-González, C. and Prado-Barragán, L.A. (2011) Purification and Characterization of a Thermodynamic Stable Serine Protease from Aspergillus fumigatus. Process Biochemistry, 46, 2001-2006.
https://doi.org/10.1016/j.procbio.2011.07.013

has been cited by the following article:

• TITLE: Novel Protease from Aspergillus tamarii URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation

  AUTHORS: Osmar Soares da Silva, Rodrigo Lira de Oliveira, Cristina Maria Souza-Motta, Ana Lúcia Figueiredo Porto, Tatiana Souza Porto

  KEYWORDS: Protease, Aspergillus tamarii, Biochemical Characterization, Solid-State Fermentation, Agroindustrial Waste

  JOURNAL NAME: Advances in Enzyme Research, Vol.4 No.4, December 2, 2016

  ABSTRACT: This study reports the protease production from Aspergillus tamarii using agroindustrial residues as substrate for solid-state fermentation (SSF) and biochemical characterization. The highest protease production was obtained using wheat bran as substrate at 72 h fermentation with maximum proteolytic activity of 401.42 U/mL, collagenase of 243.0 U/mL and keratinase of 19.1 U/mL. The protease exhibited KM = 18.7 mg/mL and Vmax = 28.5 mg/mL/min. The optimal pH was 8.0 and stable in a wide pH range (5.0 - 11.0) during 24 h. The optimum temperature was 40°C. The proteolytic activity was inhibited by Cu2+ (33.98%) and Hg2+ (22.69%). The enzyme was also inhibited by PMSF (65.11%), indicating that is a Serine Protease. These properties suggest that alkaline protease from A. tamarii URM4634 is suitable for application in food industries and leather processing. Additionally, the present findings opened new vistas in the utilization of wheat bran and other effective agroindustrial wastes as substrates for SSF.