Purification and Properties of Xylanase from Aspergillus usamii

Abstract

Abstract: A xylanase from solid-state fermentation culture of Aspergillus usamii E001 was purified by with water extraction; ammonium sulfate precipitation; and Phenyl-Sepharose CL-4B, Sephadex G-75 and DEAE-Sepharose fast flow column chromatographies. A purified xylanase, showing a single band on SDS-PAGE, was obtained with specific enzyme activity of 3047IU/mg. The molecular weight of the xylanase was determined as 23.2kD on SDS-PAGE and 23.0kD by gel filtration, indicating the xylanase as a monomer. The optimum temperature and pH value for extracting this enzyme were 50℃ and 4.6, respectively. Its kinetics coefficients Km and Vmax with oat spelt xylan as substrate were 5.27mg/ml and 6494mmol/(min·mg), respectively. Its activity was activated by Ca2+ and EDTA, while strongly activated by Sn2+、Pb2+ and Fe3+.

Key words: Aspergillus usamii, xylanase, purification, enzymatic properties

FU Dan-Dan, LI Ai-Jiang, XIE Hui, WU Min-Chen. Purification and Properties of Xylanase from Aspergillus usamii[J]. FOOD SCIENCE, 2006, 27(2): 116-120.

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Purification and Properties of Xylanase from Aspergillus usamii

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