Purification and characterization of a high molecular weight endoxylanasefrom the solid-state culture of an alkali-tolerant Aspergillus fumigatus MKU1 |
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Authors: | S. Thiagarajan M. Jeya P. Gunasekaran |
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Affiliation: | (1) Department of Genetics, School of Biological Sciences, Madurai Kamaraj University, 625021 Madurai, India |
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Abstract: | Summary A high molecular weight endoxylanase (XylF2) from the solid state culture of Aspergillus fumigatus MKU1 was purified to homogeneity by a combination of tube gel electrophoresis and electroelution methods. The purity was demonstrated by SDS-PAGE and the molecular mass of the XylF2 was found to be 66 kDa. The optimal pH and temperature for activity were 5.0 and 90 °C, respectively. The apparent K m and V max values of XylF2 with oat spelt xylan as substrate were 1.6 mg/ml and 3.25 mmol/min/mg protein respectively. The enzyme showed high activity towards oat spelt xylan while negligible activity was observed on carboxymethylcellulose. The activity of XylF2 was strongly inhibited by Hg2+, Ni2+, Zn2+, SDS and N-bromosuccinimide and stimulated by l-cysteine and iodoacetamide. The hydrolysis of oat spelt xylan by XylF2 released only xylo-oligosaccharides. |
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Keywords: | Aspergillus fumigatus biochemical characterization purification solid state culture xylanase |
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