Synergistic xylan decomposition by a reducing-end xylose-releasing exo-oligoxylanase with other xylanolytic enzymes derived from Paenibacillus xylaniclasticus strain TW1.
Paenibacillus xylaniclasticus strain TW1 is a promising tool for decomposing xylan-containing lignocellulosic biomass, since this strain possesses various genes encoding cellulolytic/hemicellulolytic enzymes. In this study, Px Rex8A from the TW1 strain was found to be a reducing-end xylose-releasing exo-oligoxylanase of glycoside hydrolase family 8, which cleaves xylose from xylooligosaccharides of corn core xylan. In a synergistic assay, the efficient decomposition of oat spelt xylan (OSX) and beech wood xylan was exemplified in the combination of endo-β-1,4-xylanase (Px Xyn11A) and Px Rex8A from the TW1 strain in a molar ratio of 4:1. Furthermore, it was found that the addition of β- d -xylosidase/α- l -arabinofuranosidase (Px Xyl43A) from this strain with Px Xyn11A and Px Rex8A achieved twice the amount of reducing sugars (1.1 mg/mL) against OSX after 24 h compared to Px Xyn11A alone (0.5 mg/mL). These results demonstrate that synergy effect of Px Rex8A and Px Xyl43A with Px Xyn11A promotes xylan degradation into xylose.