Multifunctional properties of glycoside hydrolase family 43 from Paenibacillus curdlanolyticus strain B-6 including exo-β-xylosidase, endo-xylanase, and α-L-arabinofuranosidase activities
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Author list: Wongratpanya K., Imjongjairak S., Waeonukul R., Sornyotha S., Phitsuwan P., Pason P., Nimchua T., Tachaapaikoon C., Ratanakhanokchai K.
Publisher: North Carolina State University
Publication year: 2015
Journal: BioResources (1930-2126)
Volume number: 10
Issue number: 2
Start page: 2492
End page: 2505
Number of pages: 14
ISSN: 1930-2126
Languages: English-Great Britain (EN-GB)
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Abstract
The glycoside hydrolase family 43 from Paenibacillus curdlanolyticus strain B-6 (GH43B6) exhibited multifunctional properties, including exo-β-xylosidase, endo-xylanase, and α-L-arabinofuranosidase enzymatic activities. GH43B6 released xylose as a hydrolysis product from the successive reduction of xylooligosaccharides as a result of exo-β-xylosidase activity. Moreover, GH43B6 also predominantly released xylose from low-substituted xylan derived from birchwood. However, when the highly substituted rye flour arabinoxylan was used as a substrate, exo-β-xylosidase activity changed to endo-xylanase activity, indicating that the enzymatic property of GH43B6 is influenced by the substituted side groups of xylan. For α-L-arabinofuranosidase, arabinose was released from short-chain substrates including p-nitrophenyl-α-L-arabinofuranoside and α-L-Araf-(1→2)-[α-L-Araf-(1→3)]-β-D-Xylp. This study reports the novel trifunctional properties of GH43B6 containing exo- and endo-activity together with xylanolytic debranching enzymatic activity, which increases its potential for application in lignocellulose-based biorefineries.
Keywords
Exo-β-xylosidase/endo-xylanase/α-L-arabinofuranosidase activities
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