The GH67 _-glucuronidase of Paenibacillus curdlanolyticus B-6 removes hexenuronic acid groups and facilitates biodegradation of the model xylooligosaccharide hexenuronosyl xylotriose
dc.contributor.author | Krisna Septiningrum | |
dc.contributor.author | Hiroshi Ohi | |
dc.contributor.author | Rattiya Waeonukul | |
dc.contributor.author | Patthra Pason | |
dc.contributor.author | Chakrit Tachaapaikoon | |
dc.contributor.author | Khanok Ratanakhanokchai | |
dc.contributor.author | Junjarus Sermsathanaswadi | |
dc.contributor.author | Lan Deng | |
dc.contributor.author | Panida Prawitwong | |
dc.contributor.author | Akihiko Kosugi | |
dc.date.accessioned | 2025-03-10T07:36:30Z | |
dc.date.available | 2025-03-10T07:36:30Z | |
dc.date.issued | 2015 | |
dc.description.abstract | 4-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. | |
dc.identifier.citation | Enzyme and Microbial Technology | |
dc.identifier.doi | 10.1016/j.enzmictec.2015.01.006 | |
dc.identifier.issn | 1410229 | |
dc.identifier.scopus | 2-s2.0-84923059877 | |
dc.identifier.uri | https://repository.dusit.ac.th//handle/123456789/4843 | |
dc.language | English | |
dc.publisher | Elsevier Inc. | |
dc.rights.holder | Scopus | |
dc.subject | GH67 | |
dc.subject | Hexenuronic acid | |
dc.subject | Hexenuronosyl xylotriose | |
dc.subject | Paenibacillus curdlanolyticus | |
dc.subject | _-Glucuronidase | |
dc.title | The GH67 _-glucuronidase of Paenibacillus curdlanolyticus B-6 removes hexenuronic acid groups and facilitates biodegradation of the model xylooligosaccharide hexenuronosyl xylotriose | |
dc.type | Article | |
mods.location.url | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84923059877&doi=10.1016%2fj.enzmictec.2015.01.006&partnerID=40&md5=a55d072b32a134fb4bcb678358cb07f4 | |
oaire.citation.endPage | 35 | |
oaire.citation.startPage | 28 | |
oaire.citation.volume | 71 |