Magnetic graphene oxide as a platform for the immobilization of cellulases and xylanases: Ultrastructural characterization and assessment of lignocellulosic biomass hydrolysis

Cedeño, Fernando Roberto Paz; Carceller, Jose Miguel; Iborra, Sara; Donato, Ricardo K.; Godoy, Anna Paula; Paula, Ariela Veloso de; Monti, Rubens; Corma, Avelino; Masarin, Fernando

doi:10.1016/j.renene.2020.09.059

Cited by 69 publications

(29 citation statements)

References 72 publications

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“…Although immobilized DIOMNP and GLA derivatives showed loss of specific activity after reduction with NaBH 4 , the results obtained in this work are similar and promising when compared to the results of other works published in the literature. Paz-Cedeno et al [27] studied the immobilization of endocellulase and β-glucosidase on graphite oxidemagnetite reaching 63.4% and 97.2% of immobilization respectively. Endocellulase from Scytalidium thermophilum and β-glucosidase from Humicola insolens were immobilized on magnetic nanoparticles with chitosan activated with NiCl 2 , reaching a 20% immobilization yield for both enzymes [28].…”

Section: Immobilization Of Endocellulase and β-Glucosidase On Different Supportsmentioning

confidence: 99%

“…Studies about immobilization of endocellulase and β-glucosidase on different supports and applying different strategies show the possibility to reuse of immobilized derivatives, conserving between 40 and 90% of the initial enzymatic activity. Among the several studies reported, recently Paz-Cedeno et al [27] used graphite oxide-magnetite to immobilize endocellulase and β-glucosidase resulting in stable derivatives capable of maintaining 70% and 88% of their initial enzymatic activities, respectively, after 10 cycles of reuse. Abraham et al [32] immobilized cellulases on magnetite nanoparticles using glutaraldehyde resulting in a stable derivative capable of maintaining 70% of its initial enzymatic activity after 10 consecutive hydrolysis cycles.…”

Section: Derivatives Reusementioning

confidence: 99%

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

et al. 2021

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The 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.

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Section: Immobilization Of Endocellulase and β-Glucosidase On Different Supportsmentioning

confidence: 99%

Section: Derivatives Reusementioning

confidence: 99%

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

et al. 2021

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“…Even so, the reuse of these immobilized biocatalysts was possible for eight cycles with less than 25% activity reduction, except for xylanase, which lost about 30% of its activity. Furthermore, the hydrolysis of sugarcane bagasse pretreated with xylose was maintained with a 78% yield until the fifth cycle, but the glucose yield was lowered by 34% after five cycles [55]. In this context, immobilized xylanase in activated MNPs using EDC as a coupling agent and grafting to GO is a promising route for xylan saccharification and recyclability of its bioactivity.…”

Section: Immobilization and Co-immobilization Of Hemicellulose-degrading Enzymesmentioning

confidence: 99%

Magnetic Nanomaterials as Biocatalyst Carriers for Biomass Processing: Immobilization Strategies, Reusability, and Applications

2021

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Environmental concerns, along with oil shortages, have increased industrial interest in biomass conversion to produce biofuels and other valuable chemicals. A green option in biomass processing is the use of enzymes, such as cellulases, hemicellulases, and ligninolytic (laccase and peroxidases), which have outstanding specificity toward their substrates and can be reused if immobilized onto magnetic nanocarriers. Numerous studies report the biocatalysts’ performance after covalent binding or adsorption on differently functionalized magnetic nanoparticles (MNPs). Functionalization strategies of MNPs include silica-based surfaces obtained through a sol–gel process, graphene oxide-based nanocomposites, polymer-coated surfaces, grafting polymer brushes, and others, which have been emphasized in this review of the immobilization and co-immobilization of enzymes used for biomass conversion. Careful analysis of the parameters affecting the performance of enzyme immobilization for new hybrid matrices has enabled us to achieve wider tolerance to thermal or chemical stress by these biosystems during saccharification. Additionally, it has enabled the application of immobilized laccase to remove toxic organic compounds from lignin, among other recent advances addressed here related to the use of reusable magnetic carriers for bioderived chemical manufacturing.

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“…The results indicated that by increasing temperature, endothermal process was occurred, which resulted high cellulase adsorption. Similarly, Paz-Cedeno et al [85] studied the immobilization of cellulase and xylanase enzymes using graphene oxide-magnetic nanoparticles (GO-MNPs) as support-material for efficient synthesis of cellulosic ethanol and other useful compounds. Homogeneous distribution of MNPs onto the graphene oxide nanosheets was observed.…”

Section: Cellulases Immobilization On Non-magnetic Magnetic Nanostruc...mentioning

confidence: 99%

Cellulose-deconstruction potential of nano-biocatalytic systems: A strategic drive from designing to sustainable applications of immobilized cellulases

Qamar

Bilal

et al. 2021

International Journal of Biological Macromolecules

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Magnetic graphene oxide as a platform for the immobilization of cellulases and xylanases: Ultrastructural characterization and assessment of lignocellulosic biomass hydrolysis

Cited by 69 publications

References 72 publications

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

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

Magnetic Nanomaterials as Biocatalyst Carriers for Biomass Processing: Immobilization Strategies, Reusability, and Applications

Cellulose-deconstruction potential of nano-biocatalytic systems: A strategic drive from designing to sustainable applications of immobilized cellulases

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