Production, purification and characterization of tannase from Aspergillus tamarii

• Published in: African journal of biotechnology Vol. 11; no. 2; pp. 391 - 398
• Main Authors: da Costa, AM, Kadowaki, M K, Minozzo, M C, de Souza, CGM, Boer, C G, Bracht, A, Peralta, R M
• Format: Journal Article
• Language: English
• Published: 05.01.2012
• Subjects: Aspergillus tamarii
• ISSN: 1684-5315; 1684-5315
• DOI: 10.5897/AJB11.1752

The production of tannases by Aspergillus tamarii was evaluated in submerged cultures using tannic acid and gallic acid as substrates. Two tannases, designated as TAH I and TAH II were produced in gallic acid submerged cultures. TAH I, responsible for 70% of the total tannase activity was purified to apparent electrophoretic homogeneity with 18.35% yield. The enzyme is a homodimeric protein with molecular mass of 180 kDa and 40.5% of its weight corresponds to carbohydrates. TAH I exhibited optimal activity at 30 degree C and pH 5.5 and was stable over a large pH range (3.0 to 9.0) and at temperatures up to 40 degree C. With methyl gallate as substrate, the enzyme presented a K sub(M) of 0.77 mM and a V sub(max) of 682.8 U/mg proteins. The enzyme was inhibited by metal ions but showed relative resistance to organic solvents and surfactants. Since the enzyme is active over a wide range of pH and temperature, it is potentially useful in food and pharmaceutical industries.