کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
17506 | 42673 | 2011 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Chrysosporium lucknowense C1 arabinofuranosidases are selective in releasing arabinose from either single or double substituted xylose residues in arabinoxylans Chrysosporium lucknowense C1 arabinofuranosidases are selective in releasing arabinose from either single or double substituted xylose residues in arabinoxylans](/preview/png/17506.png)
Two novel arabinofuranosidases, Abn7 and Abf3 from Chrysosporium lucknowense (C1), belonging to the glycoside hydrolase family 43 and 51 were purified and characterized. Abn7 is exclusively able to hydrolyze arabinofuranosyl residues at position O-3 of double substituted xylosyl residues in arabinoxylan-derived oligosaccharides, an activity rarely found thus far. Abf3 is able to release arabinose from position O-2 or O-3 of single substituted xyloses. Both enzymes performed optimal at pH 5.0 and 40 °C.Combining Abn7 and Abf3 resulted in a synergistic increase in arabinose release from arabinoxylans. This synergistic effect is due to the action of Abf3 on the remaining arabinose residues at position O-2 on single substituted xylosyl residues resulting from the action of Abn7 on double substituted xylosyl residues. Arabinose release was further increased when an endo-1,4-β-xylanase was present during digestion. The efficiency of these arabinohydrolases from C1 on insoluble arabinoxylan substrates is discussed.
Journal: Enzyme and Microbial Technology - Volume 48, Issues 4–5, 7 April 2011, Pages 397–403