The family 22 carbohydrate-binding module of bifunctional xylanase/_-glucanase Xyn10E from Paenibacillus curdlanolyticus B-6 has an important role in lignocellulose degradation

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dc.contributor.authorJunjarus Sermsathanaswadi
dc.contributor.authorSirilak Baramee
dc.contributor.authorChakrit Tachaapaikoon
dc.contributor.authorPatthra Pason
dc.contributor.authorKhanok Ratanakhanokchai
dc.contributor.authorAkihiko Kosugi
dc.contributor.correspondenceA. Kosugi; Biological Resources and Post-harvest Division, Japan International Research Center for Agricultural Sciences (JIRCAS), Tsukuba, 1-1 Ohwashi, 305-8686, Japan; email: akosugi@affrc.go.jp
dc.date.accessioned2025-03-10T07:36:30Z
dc.date.available2025-03-10T07:36:30Z
dc.date.issued2017
dc.description.abstractA newly isolated endo-_-1,4-xylanase (Xyn10E) from Paenibacillus curdlanolyticus B-6 has a modular structure consisting of a family 22 carbohydrate-binding module (CBM), a glycoside hydrolase (GH) family 10 catalytic domain, two fibronectin type III (Fn3) domains, and a family 3 CBM at the C-terminus. Intact Xyn10E (rXyn10E), CBM22-deleted Xyn10E (X-CBM3), CBM3-deleted Xyn10E (X-CBM22), and GH10 catalytic domain only (X-GH10) were expressed in Escherichia coli. rXyn10E showed bifunctional degradation activity toward xylan and _-glucan and also degraded microcrystalline cellulose. Although X-CBM3 and X-GH10 had drastically reduced xylanase and _-glucanase activities, X-CBM22 mostly retained these activities. Similar Km values were obtained for rXyn10E and X-CBM3, but kcat and kcat/Km values for X-CBM3 and X-GH10 were lower than those for rXyn10E, suggesting that CBM22 of Xyn10E may contribute to catalytic efficiency. In binding assays, X-CBM3 was still able to bind to _-glucan, soluble xylan, insoluble xylan, and cellulose through GH10 and CBM3. These results indicate that CBM22 has an important role not only in binding to xylan and _-glucan but also in feeding both polysaccharides into the neighboring GH10 catalytic domain. rXyn10E showed remarkable synergism with rXyn11A, a major xylanase subunit of P. curdlanolyticus B-6, in the degradation of untreated corn stover and sugarcane bagasse; however, the combination of X-CBM3 and rXyn11A was not synergistic. These results indicate that Xyn10E and Xyn11A act synergistically on lignocellulosic biomass, and CBM22 is essential for efficient degradation of lignocellulosic materials. � 2016 Elsevier Inc.
dc.identifier.citationEnzyme and Microbial Technology
dc.identifier.doi10.1016/j.enzmictec.2016.09.015
dc.identifier.issn1410229
dc.identifier.scopus2-s2.0-84990866300
dc.identifier.urihttps://repository.dusit.ac.th//handle/123456789/4810
dc.languageEnglish
dc.publisherElsevier Inc.
dc.rights.holderScopus
dc.subjectBifunctional
dc.subjectCBM22
dc.subjectGH10
dc.subjectPaenibacillus curdlanolyticus
dc.subjectXylanase
dc.subject_-Glucanase
dc.titleThe family 22 carbohydrate-binding module of bifunctional xylanase/_-glucanase Xyn10E from Paenibacillus curdlanolyticus B-6 has an important role in lignocellulose degradation
dc.typeArticle
mods.location.urlhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84990866300&doi=10.1016%2fj.enzmictec.2016.09.015&partnerID=40&md5=8eb9132e752598cfd8babbb41dab3baf
oaire.citation.endPage84
oaire.citation.startPage75
oaire.citation.volume96
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