Kinetic modeling of cellobiose by a β-glucosidase from Aspergillus fumigatus

Wojtusik, Mateusz; Yepes, Clara M.; Villar, Juan C.; Cordes, Arno; Arroyo, Miguel; Garcı́a-Ochoa, Félix; Ladero, Miguel

doi:10.1016/j.cherd.2018.06.020

Cited by 14 publications

(14 citation statements)

References 35 publications

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“…Combining both results, a specific activity of 15.2 U_ pNPG /mg protein was obtained. This activity value agrees with that reported by other authors for this ASA-1000 β-glucosidase formulation [33].…”

Section: Design Of Immobilized Preparations Of β-Glucosidasesupporting

confidence: 93%

“…In other words, when the concentration of product in the reaction medium increases, reaction rate sharply decreases, accentuating this behavior as the substrate concentration decreases (which is a sign of competitive inhibition by product) [36]. This behavior reproduces the previously described [33] intrinsic kinetic pattern of the catalysts by the free β−glucosidases. To study this intrinsic kinetic behavior, experiments with the free enzyme batch reactors were performed under the same conditions (Figures S1 and S2, Supplementary Materials) and experimental data for free enzyme were fitted to a kinetic model of substrate-competitive inhibition and product-competitive dual inhibition and different parameters kinetic were obtained (Figure S2, Supplementary Materials).…”

Section: Implementation Of the Hydrolysis In Discontinuous Stirred Tank Reactor: Identification Of Substrate And Product Inhibitionsupporting

confidence: 79%

“…They tested it for different biocatalyst concentration, different initial substrate, and product concentration in the reaction media. The kinetic model that they propose explains the kinetic through a mixed inhibition model which involves an uncompetitive inhibition by the substrate and double competitive inhibition exerted by the product [33]. Regarding stability, given the natural function of the enzyme of working in the proximity of macromolecular substrates, operational stability might significantly differ from the one studied under resting conditions, using the free enzyme as a standard comparison.…”

Section: Introductionmentioning

confidence: 99%

“…Regarding stability, given the natural function of the enzyme of working in the proximity of macromolecular substrates, operational stability might significantly differ from the one studied under resting conditions, using the free enzyme as a standard comparison. Therefore, every solid-supported enzyme formulation has to be specifically addressed regarding kinetic and stability [10,18,[33][34][35].…”

Section: Introductionmentioning

confidence: 99%

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Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

Alvarez-Gonzalez¹,

Santos²,

Ladero³

et al. 2022

Catalysts

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Cellulose saccharification to glucose is an operation of paramount importance in the bioenergy sector and the chemical and food industries, while glucose is a critical platform chemical in the integrated biorefinery. Among the cellulose degrading enzymes, β-glucosidases are responsible for cellobiose hydrolysis, the final step in cellulose saccharification, which is usually the critical bottleneck for the whole cellulose saccharification process. The design of very active and stable β-glucosidase-based biocatalysts is a key strategy to implement an efficient saccharification process. Enzyme immobilization and reaction engineering are two fundamental tools for its understanding and implementation. Here, we have designed an immobilized-stabilized solid-supported β−glucosidase based on the glyoxyl immobilization chemistry applied in porous solid particles. The biocatalyst was stable at operational temperature and highly active, which allowed us to implement 25 °C as working temperature with a catalyst productivity of 109 mmol/min/gsupport. Cellobiose degradation was implemented in discontinuous stirred tank reactors, following which a simplified kinetic model was applied to assess the process limitations due to substrate and product inhibition. Finally, the reactive process was driven in a continuous flow fixed-bed reactor, achieving reaction intensification under mild operation conditions, reaching full cellobiose conversion of 34 g/L in a reaction time span of 20 min.

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Section: Design Of Immobilized Preparations Of β-Glucosidasesupporting

confidence: 93%

Section: Implementation Of the Hydrolysis In Discontinuous Stirred Tank Reactor: Identification Of Substrate And Product Inhibitionsupporting

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

Alvarez-Gonzalez¹,

Santos²,

Ladero³

et al. 2022

Catalysts

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“…In addition, BGL synthesized a number of β-glucosides, abioflavanoid molecules that bond to glucose and are considered a subtype of glycosidase in plants. Additionally, because of its involvement in fundamental biological processes, multiple reports on its potential applications have been documented by the researchers, such as the hydrolysis of glucosyl ceramides in mammals and humans [95,96], the formation of glycoconjugates that play role in the defense mechanism of plants and microbes [24]. Beta-glucosidase acts on the precursors of glucosides found in fruits, and helps in the removal of aromatic compounds [97].…”

Section: Industrial Importance Of β-Glucosidase In Biofuelsmentioning

confidence: 99%

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

et al. 2019

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The biomass to biofuels production process is green, sustainable, and an advanced technique to resolve the current environmental issues generated from fossil fuels. The production of biofuels from biomass is an enzyme mediated process, wherein β-glucosidase (BGL) enzymes play a key role in biomass hydrolysis by producing monomeric sugars from cellulose-based oligosaccharides. However, the production and availability of these enzymes realize their major role to increase the overall production cost of biomass to biofuels production technology. Therefore, the present review is focused on evaluating the production and efficiency of β-glucosidase enzymes in the bioconversion of cellulosic biomass for biofuel production at an industrial scale, providing its mechanism and classification. The application of BGL enzymes in the biomass conversion process has been discussed along with the recent developments and existing issues. Moreover, the production and development of microbial BGL enzymes have been explained in detail, along with the recent advancements made in the field. Finally, current hurdles and future suggestions have been provided for the future developments. This review is likely to set a benchmark in the area of cost effective BGL enzyme production, specifically in the biorefinery area.

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Chemical Reaction Engineering to Understand Applied Kinetics in Free Enzyme Homogeneous Reactors

Lorente-Arevalo

García-Martín

Ladero

et al. 2021

Methods in Molecular Biology

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Kinetic modeling of cellobiose by a β-glucosidase from Aspergillus fumigatus

Cited by 14 publications

References 35 publications

Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

Chemical Reaction Engineering to Understand Applied Kinetics in Free Enzyme Homogeneous Reactors

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