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Purification and characterization of a thermostable cellulase-free xylanase from the newly isolated Paecilomyces themophila

Paper ID Volume ID Publish Year Pages File Format Full-Text
18395 42721 2006 8 PDF Available
Title
Purification and characterization of a thermostable cellulase-free xylanase from the newly isolated Paecilomyces themophila
Abstract

The newly isolated thermophilic fungus, Paecilomyces themophila J18, when grown on a medium containing corncob (4%, w/v) at 50 °C for 5 days, produced 1470 U ml−1 of xylanase. Xylanase was purified 2.4-fold to homogeneity with a recovery yield of 38.3%. It appeared as a single protein band on SDS-PAGE gel with a molecular mass of approximately 25.8 kDa. The xylanase was a glycoprotein with a neutral carbohydrate content of 21.0%. It had an optimum pH of 7.0, and was stable over pH 6.0–11.0. The optimal temperature of the xylanase was 75–80 °C and it was stable up to 75 °C at pH 7.0. Apparent Km values of the xylanase for birchwood, beechwood, soluble and insoluble oat-spelt xylans were 1.6, 2.4, 2.0 and 11.8 mg ml−1, respectively. The xylanase hydrolyzed beechwood xylan and xylooligosaccharides to yield mainly xylotriose and xylobiose as end products, suggesting it is an endo-xylanase. This is the first report on the purification and characterization of a thermostable xylanase from Paecilomyces themophila. These findings in this study have great implications for the future applications of the xylanase.

Keywords
BSA, bovine serum albumin; CAPS, (cyclohexylamino)-1-propanesulphonic acid; CHES, 2-(cyclohexylamino)ethanesulphonic acid; CMC, carboxymethylcellulose; DNS, dinitrosalicylic acid; EDTA, ethylenediaminetetracetic acid; MOPS, 3-(N-morpholino)-propane sulpho
First Page Preview
Purification and characterization of a thermostable cellulase-free xylanase from the newly isolated Paecilomyces themophila
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 38, Issue 6, 1 April 2006, Pages 780–787
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering