Preparation and Properties of High Activity Tannase with Aspergillus niger T3-5-1
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Abstract:
Tannase was produced by Aspergillus niger T3-5-1, then the crude enzyme was preliminary purified by ammonium sulfate precipitation and dialysis respectively. The results showed that, specific activity of the crude enzyme dealed with dialysis sack of 12 kDa MWCO was higher than that of ammonium sulfate precipitation. Further purification was performed by Sephadex G-100 dextran gel chromatography, and then high purity tannase was obtained. Compared the tannase with Tannase A and Tannase B by GPC chromatogram, it was found that their molecular weight were generally consistent. However, specific activity of the tannase(5304.78 U/mg) was far higher than those of Tannase A (1788.15 U/mg) and Tannase B (935.07 U/mg). The optimum pH and reaction temperature of the tannase were 5.0 and 45 ℃, respectively,, with favorable pH and thermal stability. When the substrate, the Vmax and Km were were propyl gallate (PG), 81.96 μmol/(L?min) and 0.85 mmol/L, respectively. At last, the catalytic synthesis ability of the tannase was investigated, which suggested that the enzyme could catalyze the reaction between gallic acid and propyl alcohol to synthesize PG in the reverse micelle of AOT- isooctane.
