Xylan-specific carbohydrate-binding module belonging to family 6 enhances the catalytic performance of a GH11 endo-xylanase

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dc.creatorZaira Bruna Hoffmam
dc.creatorLeticia Maria Zanphorlin
dc.creatorJúnio Cota Silva
dc.creatorJosé Alberto Diogo
dc.creatorGabriela Berthou de Almeida
dc.creatorAndré Ricardo de Lima Damásio
dc.creatorFábio Márcio Squina
dc.creatorMario Tyago Murakami
dc.creatorRoberto Ruller
dc.date.accessioned2023-04-27T18:35:45Z
dc.date.accessioned2025-09-08T23:31:08Z
dc.date.available2023-04-27T18:35:45Z
dc.date.issued2016
dc.identifier.doihttp://dx.doi.org/10.1016/j.nbt.2016.02.006
dc.identifier.issn1871-6784
dc.identifier.urihttps://hdl.handle.net/1843/52602
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofNew Biotechnology
dc.rightsAcesso Restrito
dc.subjectCarboidratos
dc.subjectCatalisadores
dc.subjectEnzimas
dc.subject.otherCarboidratos
dc.subject.otherCatalisadores
dc.subject.otherEnzimas
dc.titleXylan-specific carbohydrate-binding module belonging to family 6 enhances the catalytic performance of a GH11 endo-xylanase
dc.typeArtigo de periódico
local.citation.epage472
local.citation.issue4
local.citation.spage467
local.citation.volume33
local.description.resumoXylanases catalyze the hydrolysis of b-1,4-linked xylosyl moieties from xylan chains, one of the most abundant hemicellulosic polysaccharides found in plant cell walls. These enzymes can exist either as single catalytic domains or as modular proteins composed of one or more carbohydrate-binding modules (CBMs) appended to the catalytic core. However, the molecular mechanisms governing the synergistic effects between catalytic domains and their CBMs are not fully understood. Thus, the goal of this study was to evaluate the functional effects of the fusion of a CBM belonging to family 6, which exhibits high affinity to xylan, with the GH11 xylanase from Bacillus subtilis, which does not have a CBM in its wild-type form. The wild-type enzyme (BsXyl11) and the chimeric protein (BsXyl11-CBM6) were heterologously produced in Escherichia coli and purified to homogeneity for biochemical characterization. The molecular fusion did not alter the pH and temperature dependence, but kinetic data revealed an increase of 65% in the catalytic efficiency of the chimeric enzyme. Furthermore, the BsXyl11-CBM6 chimera was used to supplement the commercial cocktail Accellerase1 1500 and improved the reducing sugar release by 17% from pretreated sugarcane bagasse. These results indicate that CBM6 can be used as a molecular tool to enhance the catalytic performance of endo-xylanases (GH11) and provide a new strategy for the development of optimized biocatalysts for biotechnological applications.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG

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