Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/5595
Title: Purification and characterization of an endoxylanase from solid-state culture of alkalitolerant <i style="">Aspergillus fumigatus</i> MKU1
Authors: Thiagarajan, S
Jeya, M
Gunasekaran, P
Keywords: <i style="">Aspergillus fumigatus</i>
biochemical characterization
purification
solid state culture
xylanase
Issue Date: Jul-2006
Publisher: CSIR
Series/Report no.: Int. Cl.<sup>8</sup> C12N9/42; C12R1/68
Abstract: A novel high molecular weight endoxylanase (XylF1) from the solid state culture of <i style="">Aspergillus fumigatus</i> 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 <i style="">p</i>H and temperature for enzyme activity were 7.0 and 70°<sup> </sup>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 <sup>2+</sup>, Cu <sup>2+</sup>, Fe<sup>3+</sup> and NBS, whereas stimulated by DTT, DTNB and L-Cysteine. The hydrolysis of oat spelt xylan released only xylooligosaccharides.
Description: 351-356
URI: http://hdl.handle.net/123456789/5595
ISSN: 0975-0967 (Online); 0972-5849 (Print)
Appears in Collections:IJBT Vol.05(3) [July 2006]

Files in This Item:
File Description SizeFormat 
IJBT 5(3) 351-356.pdf286.3 kBAdobe PDFView/Open


Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.