Biochemical and thermodynamic characteristics of a new serine protease from URM 4133.

A protease from the fungus URM 4133, capable of producing bioactive peptides from goat casein, was purified. SDS-PAGE and zymography showed a molecular mass of 30 kDa. The enzyme was active and stable in a wide pH range (6.

Application of aqueous biphasic systems as strategy to purify tannase from Aspergillus tamarii URM 7115.

The aims of the current study are to assess the influence of polyethylene glycol (PEG) concentration, molar mass, pH, and citrate concentrations on aqueous biphasic systems based on 2 factorial designs, as well as to check their capacity to purify tannase secreted by Aspergillus tamarii URM 7115. Tannase was produced through submerged fermentation at 26°C for 67 h in Czapeck-Dox modified broth and added with yeast extract and tannic acid. The factorial design was followed to assess the influence of PEG molar mass (M 600; 4,000 and 8,000 g/ mol), and PEG (C 20.