Krisna SeptiningrumHiroshi OhiRattiya WaeonukulPatthra PasonChakrit TachaapaikoonKhanok RatanakhanokchaiJunjarus SermsathanaswadiLan DengPanida PrawitwongAkihiko Kosugi2025-03-102025-03-102015Enzyme and Microbial Technology141022910.1016/j.enzmictec.2015.01.0062-s2.0-84923059877https://repository.dusit.ac.th//handle/123456789/48434-O-Methylglucuronic acid (MeGlcA) side groups attached to the xylan backbone through _-1,2 linkages are converted to hexenuronic acid (HexA) during alkaline pulping. _-Glucuronidase (EC 3.2.1.139) hydrolyzes 1,2-linked MeGlcA from xylooligosaccharides. To determine whether _-glucuronidase can also hydrolyze HexA-decorated xylooligosaccharides, a gene encoding _-glucuronidase (AguA) was cloned from Paenibacillus curdlanolyticus B-6. The purified protein degraded hexenuronosyl xylotriose (_X3), a model substrate prepared from kraft pulp. AguA released xylotriose and HexA from _X3, but the Vmax and kcat values for _X3 were lower than those for MeGlcA, indicating that HexA side groups may affect the hydrolytic activity. To explore the potential for biological bleaching, _X3 degradation was performed using intracellular extract from P. curdlanolyticus B-6. The intracellular extract, with synergistic _-glucuronidase and _-xylosidase activities, degraded _X3 to xylose and HexA. These results indicate that _-glucuronidase can be used to remove HexA from _X3 derived from pulp, reducing the need for chemical treatments in the pulping process. � 2015 Elsevier Inc.GH67Hexenuronic acidHexenuronosyl xylotriosePaenibacillus curdlanolyticus_-GlucuronidaseArticleScopus