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|Title:||Purification and characterization of an endoxylanase from solid-state culture of alkalitolerant Aspergillus fumigatus MKU1|
solid state culture
|Series/Report no.:||Int. Cl.8 C12N9/42; C12R1/68|
|Abstract:||A novel high molecular weight endoxylanase (XylF1) from the solid state culture of Aspergillus fumigatus MKU1 strain was purified to homogeneity by a combination of tube gel electrophoresis and electroelution methods. The purity of XylF1 was demonstrated by SDS-PAGE, which has the molecular mass of 43 kDa. The optimal pH and temperature for enzyme activity were 7.0 and 70° C, respectively. Further, the apparent Km and Vmax values of XylF1 with oat spelt xylan as substrate were 6.25 mg/mL and 0.05 mmol/mL/min (2.5 mmol/min/mg protein), respectively. The enzyme showed high activity on oat spelt xylan, while only trace of activity was observed on carboxy methylcellulose. The activity of XylF1 was strongly inhibited by Hg 2+, Cu 2+, Fe3+ and NBS, whereas stimulated by DTT, DTNB and L-Cysteine. The hydrolysis of oat spelt xylan released only xylooligosaccharides.|
|ISSN:||0975-0967 (Online); 0972-5849 (Print)|
|Appears in Collections:||IJBT Vol.05(3) [July 2006]|
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