Development and Biotechnological Application of a Novel Endoxylanase Family GH10 Identified from Sugarcane Soil Metagenome

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorAlvarez, Thabata M.
dc.creatorGoldbeck, Rosana
dc.creatorSantos, Camila Ramos dos
dc.creatorPaixão, Douglas A. A.
dc.creatorGonçalves, Thiago A.
dc.creatorFranco Cairo, João Paulo L.
dc.creatorAlmeida, Rodrigo Ferreira
dc.creatorde Oliveira Pereira, Isabela
dc.creatorJackson, George
dc.creatorCota, Junio
dc.creatorBüchli, Fernanda
dc.creatorCitadini, Ana Paula
dc.creatorRuller, Roberto
dc.creatorPolo, Carla Cristina
dc.creatorde Oliveira Neto, Mario
dc.creatorMurakami, Mário T.
dc.creatorSquina, Fabio M.
dc.date2014-05-27T11:30:03Z
dc.date2016-10-25T18:51:49Z
dc.date2014-05-27T11:30:03Z
dc.date2016-10-25T18:51:49Z
dc.date2013-07-29
dc.date.accessioned2017-04-06T02:32:44Z
dc.date.available2017-04-06T02:32:44Z
dc.identifierPLoS ONE, v. 8, n. 7, 2013.
dc.identifier1932-6203
dc.identifierhttp://hdl.handle.net/11449/76069
dc.identifierhttp://acervodigital.unesp.br/handle/11449/76069
dc.identifier10.1371/journal.pone.0070014
dc.identifierWOS:000323369700119
dc.identifier2-s2.0-84880808378.pdf
dc.identifier2-s2.0-84880808378
dc.identifierhttp://dx.doi.org/10.1371/journal.pone.0070014
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/896782
dc.descriptionMetagenomics has been widely employed for discovery of new enzymes and pathways to conversion of lignocellulosic biomass to fuels and chemicals. In this context, the present study reports the isolation, recombinant expression, biochemical and structural characterization of a novel endoxylanase family GH10 (SCXyl) identified from sugarcane soil metagenome. The recombinant SCXyl was highly active against xylan from beechwood and showed optimal enzyme activity at pH 6,0 and 45°C. The crystal structure was solved at 2.75 Å resolution, revealing the classical (β/α)8-barrel fold with a conserved active-site pocket and an inherent flexibility of the Trp281-Arg291 loop that can adopt distinct conformational states depending on substrate binding. The capillary electrophoresis analysis of degradation products evidenced that the enzyme displays unusual capacity to degrade small xylooligosaccharides, such as xylotriose, which is consistent to the hydrophobic contacts at the +1 subsite and low-binding energies of subsites that are distant from the site of hydrolysis. The main reaction products from xylan polymers and phosphoric acid-pretreated sugarcane bagasse (PASB) were xylooligosaccharides, but, after a longer incubation time, xylobiose and xylose were also formed. Moreover, the use of SCXyl as pre-treatment step of PASB, prior to the addition of commercial cellulolytic cocktail, significantly enhanced the saccharification process. All these characteristics demonstrate the advantageous application of this enzyme in several biotechnological processes in food and feed industry and also in the enzymatic pretreatment of biomass for feedstock and ethanol production. © 2013 Alvarez et al.
dc.languageeng
dc.relationPLOS ONE
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectbagasse
dc.subjectglycoside hydrolase family 10
dc.subjectoligosaccharide
dc.subjectphosphoric acid
dc.subjectunclassified drug
dc.subjectxylan
dc.subjectxylan endo 1,3 beta xylosidase
dc.subjectxylobiose
dc.subjectxylooligosaccharide
dc.subjectxylose
dc.subjectxylotriose
dc.subjectbiomass
dc.subjectcapillary electrophoresis
dc.subjectcatalysis
dc.subjectcontrolled study
dc.subjectcrystal structure
dc.subjectenzymatic degradation
dc.subjectenzyme active site
dc.subjectenzyme activity
dc.subjectenzyme conformation
dc.subjectenzyme substrate complex
dc.subjectfood biotechnology
dc.subjectincubation time
dc.subjectmetagenome
dc.subjectnucleotide sequence
dc.subjectpH
dc.subjectsaccharification
dc.subjectsugarcane
dc.subjectX ray crystallography
dc.titleDevelopment and Biotechnological Application of a Novel Endoxylanase Family GH10 Identified from Sugarcane Soil Metagenome
dc.typeOtro


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