Aida M Farag
Alexandria University, Egypt
Title: Biobanking of stem cells: Purification, characterization and application of marine Aspergillus nomius GWA5 tannase
Biography
Biography: Aida M Farag
Abstract
Tannase ) EC 3.1.1.20) was produced from the culture filtrate of marine Aspergillus nomius GWA5 and purified by 75% acetone precipitation, followed by gel filtration on Sephadex G-100 and on DEAE-Sephadex A-50 ion exchange chromatography, yielding 4.48-fold of purification. The molecular weight of the purified tannase was 30kDa, determined by a sodium dodecyl sulphate polyacrylamide gel electrophoresis. The optimum pH and temperature of the purified tannase yielding the highest activity (291 U/mg protein) were 6.0 and 50ºC, respectively. Tannase stability shifted to a more acidic range (4-6). Tannase enzyme was fairly stable to heat treatment in absence of its substrate and it retained about 84.5% of its activity when treated at 80 ºC for 15 min. The effect of activators and inhibitors on tannase activity was investigated, only Mg2+activated the pure enzyme while Cd2+, EDTA, Pb2+ and Hg2+ inhibited the enzyme activity and it retained about 51.55%, 40.78%, 30.24% and 24.55% of its activity, respectively. Tannase showed promising activity in removing tannin stains of tea from clothes.