| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10235672 | Process Biochemistry | 2012 | 7 Pages |
Abstract
⺠A novel α-l-arabinofuranosidase was purified from Chaetomium species. ⺠The optimal pH and temperature of the enzyme were pH 5.0 and 70 °C, respectively. ⺠The enzyme showed high substrate specificity for the a-l-arabinofuranosyl linkage. ⺠The full-length cDNA of α-l-AFase gene (CsAra) of 1745-bp was obtained.
Keywords
2-(cyclohexylamino)ethanesulfonic acidPDAα-l-arabinofuranosidasePNPCAPSChaetomiumCHESMOPS2-(N-morpholino)ethanesulfonic acid3-(N-morpholino)-propanesulfonic acidp-nitrophenylSDS–PAGEsodium dodecyl sulfate–polyacrylamide gel electrophoresisCharacterizationMeSPurificationGene cloningglycoside hydrolase
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Qiaojuan Yan, Luo Tang, Shaoqing Yang, Peng Zhou, Shuping Zhang, Zhengqiang Jiang,