Repository logo
 
Publication

Sugarcane Bagasse Saccharification by Enzymatic Hydrolysis Using Endocellulase and β-glucosidase Immobilized on Different Supports

2021Journal article Open access
Simple item page
dc.contributor.authorMorais Júnior, Wilson Galvão
dc.contributor.authorPacheco, Thályta F.
dc.contributor.authorGao, Shipeng
dc.contributor.authorMartins, Pedro A.
dc.contributor.authorGuisán, José M.
dc.contributor.authorCaetano, Nídia
dc.date.accessioned2021-09-09T09:28:33Z
dc.date.available2021-09-09T09:28:33Z
dc.date.issued2021
dc.description.abstractThe saccharification of sugarcane bagasse by enzymatic hydrolysis is one of the most promising processes for obtaining fermentable sugar to be used in the production of second-generation ethanol. The objective of this work was to study the immobilization and stabilization of two commercial enzymes: Endocellulase (E-CELBA) in dextran coated iron oxide magnetic nanoparticles activated with aldehyde groups (DIOMNP) and β-glucosidase (E-BGOSPC) in glyoxyl agarose (GLA) so that their immobilized derivatives could be applied in the saccharification of pretreated sugarcane bagasse. This was the first time that the pretreated sugarcane bagasse was saccharified by cascade reaction using a endocellulase immobilized on dextran coated Fe2O3 with aldehyde groups combined with a β-glucosidase immobilized on glyoxyl agarose. Both enzymes were successfully immobilized (more than 60% after reduction with sodium borohydride) and presented higher thermal stability than free enzymes at 60, 70, and 80 °C. The enzymatic hydrolysis of the sugarcane bagasse was carried out with 15 U of each enzyme per gram of bagasse in a solid-liquid ratio of 1:20 for 48 h at 50 °C. Under these conditions, 39.06 ± 1.18% of the cellulose present in the pretreated bagasse was hydrolyzed, producing 14.11 ± 0.47 g/L of reducing sugars (94.54% glucose). In addition, DIOMNP endo-cellulase derivative maintained 61.40 ± 1.17% of its enzymatic activity after seven reuse cycles, and GLA β-glucosidase derivative maintained up to 58.20 ± 1.55% of its enzymatic activity after nine reuse cycles.pt_PT
dc.description.sponsorshipThe authors thank sugarcane refinery Jalles Machado S.A for the sugarcane biomass donation; This work was supported by Institute of Catalysis and Petrochemistry (ICP) belonging to the Spanish Council for Scientific Research (CSIC) and Center for Innovation in Engineering and Industrial Technology (CIETI). This research is part of the project titled ProEMiBiL supported bu European Union’s Horizon 2020 funded by Marie Skłodowska-Curie, grant number #867473. This work was financially supported by Base Funding-UIDB/04730/2020 of Center for Innovation in Engineering and Industrial Technology, CIETI-funded by national funds through the FCT/MCTES (PIDDAC); Base Funding-UIDB/0051/2020 of Laboratory for Process Engineering, Environment, Biotechnology and Energy-LEPABE-funded by National funds through the FCT/MCTES (PIDDAC).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.3390/catal11030340pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.22/18337
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationUIDB/0051/2020pt_PT
dc.relationEthanol production from microalgae and lignocellulosic biomass.
dc.relation.publisherversionhttps://www.mdpi.com/2073-4344/11/3/340pt_PT
dc.subjectEndocellulasept_PT
dc.subjectImmobilizationpt_PT
dc.subjectSaccharificationpt_PT
dc.subjectSugarcane bagassept_PT
dc.subjectβ-glucosidasept_PT
dc.titleSugarcane Bagasse Saccharification by Enzymatic Hydrolysis Using Endocellulase and β-glucosidase Immobilized on Different Supportspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleEthanol production from microalgae and lignocellulosic biomass.
oaire.awardURIinfo:eu-repo/grantAgreement/EC/H2020/867473/EU
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/157604/PT
oaire.citation.issue3pt_PT
oaire.citation.startPage340pt_PT
oaire.citation.titleCatalystspt_PT
oaire.citation.volume11pt_PT
oaire.fundingStreamH2020
oaire.fundingStream6817 - DCRRNI ID
person.familyNameMorais Júnior
person.familyNameCaetano
person.givenNameWilson Galvão
person.givenNameNídia
person.identifierR-000-DJC
person.identifier.ciencia-idA31B-7605-1668
person.identifier.ciencia-id1F1D-73E2-BFBF
person.identifier.orcid0000-0002-2530-6327
person.identifier.orcid0000-0002-2185-6401
person.identifier.ridI-3934-2012
person.identifier.scopus-author-id57193125203
person.identifier.scopus-author-id55901684900
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameEuropean Commission
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublicationca7776f6-c580-4b81-a89f-c4b3204bb028
relation.isAuthorOfPublication4bbb44e7-228a-48fb-abc2-8df5e27d0b48
relation.isAuthorOfPublication.latestForDiscovery4bbb44e7-228a-48fb-abc2-8df5e27d0b48
relation.isProjectOfPublicationab1fc27b-56e9-4bc3-bf60-579a111b315e
relation.isProjectOfPublication23ff3139-1d2c-416e-ad3e-3f2e54271bef
relation.isProjectOfPublication.latestForDiscovery23ff3139-1d2c-416e-ad3e-3f2e54271bef

Files

Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
ART12_CIETI_WilsonJr_2021.pdf
Size:
907.48 KB
Format:
Adobe Portable Document Format
Download

Collections

ISEP – CIETI – Artigos