FOOD SCIENCE ›› 2011, Vol. 32 ›› Issue (3 ): 181-185.doi: 10.7506/spkx1002-6630-201103042

• Bioengineering • Previous Articles     Next Articles

Isolation, Purification and Some Properties of Glucose Oxidase from Aspergillius niger H1-9b

SU Mo,GAO Ya-peng,LIANG Jian-rong,HUANG Jie,TANG Yun-ming   

  1. Key Laboratory of Eco-environments in Three Gorges Reservoir Region, Ministry of Education,
    Chongqing Sweetpotato Engineering Research Center, School of Life Science, Southwest University, Chongqing 400715, China
  • Received:2010-04-22 Revised:2011-01-10 Online:2011-02-15 Published:2011-01-13

Abstract: Glucose oxidase (GOD), an H2O2-producing enzyme, was isolated and purified from Aspergillius niger H1-9b through electrophoretic homogeneity, ion-exchange chromatography on DEAE-Sepharose column and Superdex-200 gel filtration chromatography. The purified GOD had a molecular weight of 94.1 kD as a monomer. The specific activity of GOD was 30569.7 U/mg with recovery rate of 30.2% and purification fold of 41.4. The optimal reaction pH and temperature of GOD were 5.7 and 37 ℃, respectively. The GOD displayed an excellent stability under the conditions of 30-40 ℃ and pH 4.0-8.0. The kinetic parameters such as Km and Vmax were 30.69 mmol/L and 21.88μmol/L while using glucose as the substrate. Obvious inhibitory effects of Ag+, Cu2+ and Zn2+ on the activity of GOD were observed. Therefore, glucose oxidase from Aspergillius niger H1-9b will have wide applications due to its excellent thermostability and stability in wide pH range.

Key words: Aspergillius niger H1-9b, glucose oxidase, isolation, purification, property

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