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Multifunctional properties of glycoside hydrolase family 43 from Paenibacillus curdlanolyticus strain B-6 including exo-β-xylosidase, endo-xylanase, and α-L-arabinofuranosidase activities
Author(s)
Wongratpanya, Kanok
Imjongjairak, Siriluck
Waeonukul, Rattiya
Phitsuwan, Paripok
Pason, Patthra
Nimchua, Thidarat
Tachaapaikoon, Chakrit
Ratanakhanokchai, Khanok
Date Issued
January 1, 2015
Type
Article
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.
Citation
Bioresources, 10(2), 2492-2505, 2015