首页 | 本学科首页   官方微博 | 高级检索  
     


Purification and biochemical characterization of an endoxylanase from Aspergillus versicolor
Authors:Eleonora Cano Carmona,Marcia Regina Brochetto-braga,Aline Aparecida Pizzirani-kleiner,Joã  o Atilio Jorge
Affiliation:Centre d'Ingénierie des Protéines, Institut de Chimie, Universitéde Liège, B6, Sart Tilman, B4000 Liège, Belgium;Laboratoire de Biochimie, Institut de Chimie, Universitéde Liège, B6, Sart Tilman, B4000 Liège, Belgium
Abstract:An endoxylanase (β-1,4-xylan xylanohydrolase, EC 3.2.1.8) was purified from the culture filtrate of a strain of Aspergillus versicolor grown on oat wheat. The enzyme was purified to homogeneity by chromatography on DEAE-cellulose and Sephadex G-75. The purified enzyme was a monomer of molecular mass estimated to be 19 kDa by SDS-PAGE and gel filtration. The enzyme was glycoprotein with 71% carbohydrate content and exhibited a pI of 5.4. The purified xylanase was specific for xylan hydrolysis. The enzyme had a K m of 6.5 mg ml−1 and a V max of 1440 U (mg protein)−1.
Keywords:β-Lactamase    Psychrophile    Secretion    Induction
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号