Purification and Characterization of Novel Bifunctional Xylanase, XynIII, Isolated from Aspergillus niger A-25
2006
Chen, H.G. (Henan Agricultural University, Zhengzhou, P. R. China), E-mail: honggeyz@163.com | Yan, Xin (Henan Agricultural University, Zhengzhou, P. R. China) | Liu, Xin Yu (Henan Agricultural University, Zhengzhou, P. R. China) | Wang, Ming Dao (Henan Agricultural University, Zhengzhou, P. R. China) | Huang, Hui Min (Henan Agricultural University, Zhengzhou, P. R. China) | Jia, Xin Cheng (Henan Agricultural University, Zhengzhou, P. R. China) | Wang, Jin An (Superior School of Chemical engineering and Industrial Extractives, National Polytechnic Institute, Mexico, Mexico)
Three types of xylanases (EC 3.2.1.8) were detected in the strain Aspergillus niger A-25, one of which, designated as XynIII, also displayed β-(l,3-1,4)-glucanase (EC 3.2.1.73) activity, as determined by a zymogram analysis. XynIII was purified by ultrafiltration and ion-exchange chromatography methods. Its apparent molecular weight was about 27.9 kDa, as estimated by SDS-PAGE. The purified XynIII could hydrolyze birchwood xylan, oat spelt xylan, lichenin, and barley β-glucan, but not CMC, avicel cellulose, or soluble starch under the assay conditions in this study.
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