Document Details

Document Type : Article In Journal 
Document Title :
Purification and characterization of acido-thermophilic xylanase from aspergillus terrus
Purification and characterization of acido-thermophilic xylanase from aspergillus terrus
 
Subject : Biological 
Document Language : English 
Abstract : Purification and characterization of extracellular xylanase from Aspergillus terrus was recorded. The enzyme was purified to homogeneity by salting out with ammonium sulphate, dialysis and passage through gel chromatography resins (Sephadex G-200, Sephadex G-100 columns) followed by anion exchange chromatography (Diethylaminoethyl Sephadex column). The purified enzyme resulted in 516.4 fold increase over the crude extract exhibited a specific activity of 175.6 unit/mg protein with the recovery of 30.6 %. Two criteria for the purity of the purified A. terrus extracellular xylanase were used. DEAE-sephadex column (final stage of purification) resulted in a single sharp peak of A. terrus pure xylanase. The second criterion was given by applying SDS-PAGE electrophoresis technique. The molecular weight of A. terrus extracellular xylanase was 33 KDa. Studying factors affecting the activity of the purified xylanase were determined. An optimum temperature and pH for the acidothermophilic purified xylanase were 50 °C at pH 4, respectively. 
ISSN : 1991-8178 
Journal Name : Australian Journal of Basic and Applied Sciences 
Volume : 5 
Issue Number : 10 
Publishing Year : 1432 AH
2011 AD 
Article Type : Article 
Added Date : Monday, April 23, 2012 

Researchers

Researcher Name (Arabic)Researcher Name (English)Researcher TypeDr GradeEmail
نيفين صالح إبراهيم جويليGeweely, Neveen S IResearcherDoctoratengeweely@yahoo.com

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