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Isolation and purification of an endoglucanase from Aspergillus niger

Zhi‐Qiang Zhang, Guo Chunteng, Lin Jiaren, Pingfan Rao

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Abstract

A novel cellulase was isolated and purified to homogeneity from a commercial Aspergillus niger cellulase preparation by a combination of ammonium sulfate and three steps of ion exchange chromatograph of CM-Sephadex C-25, DEAE-Sephadex A-50 and POROS 20 HQ. The molecular weight of the purified enzyme is 39.2?kD under reduced conditions by SDS-PAGE; the optimal pH of the enzyme is 4.0, and the optimal temperature is 55?℃, its K m is 7.41?mg/mL.

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What this paper is about

A novel cellulase was isolated and purified to homogeneity from a commercial Aspergillus niger cellulase preparation by a combination of ammonium sulfate and three steps of ion exchange chromatograph of CM-Sephadex C-25, DEAE-Sephadex A-50 and POROS 20 HQ. The molecular weight of the purified enzyme is 39.2?kD under reduced conditions by SDS-PAGE; the optimal pH of the enzyme is 4.0, and the optimal temperature is 55?℃, its K m is 7.41?mg/mL.

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Available abstract

A novel cellulase was isolated and purified to homogeneity from a commercial Aspergillus niger cellulase preparation by a combination of ammonium sulfate and three steps of ion exchange chromatograph of CM-Sephadex C-25, DEAE-Sephadex A-50 and POROS 20 HQ. The molecular weight of the purified enzyme is 39.2?kD under reduced conditions by SDS-PAGE; the optimal pH of the enzyme is 4.0, and the optimal temperature is 55?℃, its K m is 7.41?mg/mL.

Key concepts: Cellulase, Aspergillus niger, Sephadex, Ammonium sulfate, Chemistry, Chromatography, Enzyme, Hydrolysis

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