Krishnamurthy, Savita and Vithayathil, Paul Joseph (1989) Purification and characterization of endo-1,4-β-xylanase from Paecilomyces varioti Bainier. In: Journal of Fermentation and Bioengineering, 67 (2). pp. 77-82.
rification.pdf - Published Version
Restricted to Registered users only
Download (705Kb) | Request a copy
An endo-xylanase (1,4-β-d-xylanxylanohydrolase EC 18.104.22.168) was isolated from the culture filtrate of Paecilomyces varioti Bainier. The enzyme was purified 3.2 fold with a 60% yield by gel filtration and ion exchange chromatography. The purified enzyme had a molecular weight of 25,000 with a sedimentation coefficient of 2.2 S. The isoelectric point of the enzyme was 3.9. The enzyme was obtained in crystalline form. The optimum pH range was 5.5–7.0 and the temperature, 65°C. The Michaelis constant was 2.5 mg larchwood xylan/ml. The enzyme was found to degrade xylan by an endo mechanism producing arabinose, xylobiose, xylo- and arabinosylxylo-oligosaccharides, during the initial stages of hydrolysis. On prolonged incubation, xylotriose, arabinosylxylotriose and xylobiose were the major products with traces of xylotetraose, xylose and arabinose.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier science.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||26 Aug 2010 07:58|
|Last Modified:||19 Sep 2010 06:14|
Actions (login required)