Production, Purification and Physicochemical Properties of an Exo-Polygalacturonase from Aspergillus niger SW06

AUTOR(ES)

Ma, Yu-ping, Hao, Hui, Chen, Zhi-fei, Zhao, Zhi-wei, Chen, Shun-hui, Sun, Si-wen, Xu, Chun-ping

FONTE

J. Braz. Chem. Soc.

DATA DE PUBLICAÇÃO

2017-04

RESUMO

In this study, exo-polygalacturonase (exo-PG) production from Aspergillus niger SW06 was optimized by central composition design and high amount of 21.51 units mL-1 could be achieved in optimizing growth conditions. Both gel filtration and ion exchange chromatography revealed a single exo-PG activity peak, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the purified protein showed a single band with a molecular mass of 66.2 kDa. The purified enzyme exhibited maximal activity in the presence of 1% citrus pectin at the temperature of 55 ºC and pH of 5.0. The enzyme was stable within the pH range of 3.0-5.0 and below 60 ºC. The Michaelis constant (Km) and maximum velocity (Vmax) of the enzyme was found to be 0.58 mg mL-1 and 20.66 μmol (mL min)-1, respectively. The thermostable and acidic nature for the activity of this exo-PG make it possible to have wide range of industrial applications.

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