Enzyme immobilisation on wood-derived cellulose scaffolds <i>via</i> carbohydrate-binding module fusion constructs

Roberts, Aled D.; Payne, K.A.P.; Cosgrove, Sebastian C.; Tilakaratna, Viranga; Peñafiel, Itziar; Finnigan, William; Turner, Nicholas J.; Scrutton, Nigel S.

doi:10.1039/d1gc01008e

Cited by 21 publications

(11 citation statements)

References 53 publications

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“…This result implied the excellent efficiency of the immobilization method for delignified bamboo. As shown in Figure and Table S3, the protein loading capacity of the OBS (8.09 mg/m 2 ·g –1 ) is 3–20 times that of delignified wood and other cellulose-based supports with comparable or much bigger specific surface area. − Furthermore, when a high concentration of F-BSA (i.e., 1.0 mg/mL) was used, the protein loading was ∼6-fold that at low concentrations (0.1–0.4 mg/mL, Table S4 and Figure S6), indicating the diffusion rate as an important factor affecting the immobilization process. Similarly, when 1.0 mg/mL BGUs was used for immobilization, 4.4 ± 0.2 mg/g loading capacity was identified (Figure S7 and Table S4), which was close to the calculated theoretical capacity (4.8 mg/g, Table S4).…”

Section: Results and Discussionmentioning

confidence: 95%

“…Comparison of immobilized efficiency versus specific surface area of different cellulose-based systems. − BSA (MW: 66.5 kDa) was used for the measurement in this work.…”

Section: Results and Discussionmentioning

confidence: 95%

“…To date, both covalent and noncovalent strategies have been explored to immobilize enzymes on a cellulose scaffold and other solid supports. − Multiple types of interactions and multipoint interactions could occur during and after the protein immobilization, − which should be considered for the design of the immobilization method and process optimization. , The amine groups at the side chain of lysine residues and the N-terminal of the proteins are commonly used for enzyme immobilization since the majority of proteins have such amine groups on their surface, which are usually exposed to medium and accessible for derivatization . The amine group can react with the aldehyde group of the oxidized cellulose unit to form a Schiff base. , However, the Schiff base is not stable, while once reduced to the C–N bond, the formed alkylamine linkage is highly stable .…”

Section: Introductionmentioning

confidence: 99%

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Enzyme Immobilization on a Delignified Bamboo Scaffold as a Green Hierarchical Bioreactor

Ren

Zhang

Sun

et al. 2022

ACS Sustainable Chem. Eng.

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Enzymes immobilized on cellulose-based supports provide important applications because they are convenient, economical, and stable. In this paper, we report the application of delignified bamboo as a novel cellulose-based scaffold for enzyme immobilization and bamboo enzyme-based flow bioreactors, which can drastically improve the catalytic reaction and subsequent separation. The delignified bamboo provides a superior biobenign and hierarchically structured platform that can be conveniently derivatized to conjugate functional proteins with high loading capacity. With an optimized delignification process and a modified Schiff base-dependent conjugation method, we identified an efficient approach to immobilize enzymes on bamboo. In our system, generally ∼8 mg/m 2 •g −1 proteins can be immobilized on the delignified bamboo, which is significantly higher than that of the reported methods. The immobilized enzymes on bamboo showed sustained activity under ambient conditions, excellent reusability with 13 cycles, and high stability of more than 7 weeks of storage at 4 °C, which can be readily adapted in flow reactors for both single transformation and tandem catalysis. As an example, drugs of abuse in synthetic urine samples were analyzed in β-glucuronidase (BGU)-functionalized flow reactors in 0.1 M phosphate buffer, pH 7.4, at room temperature, the condition suitable for the bioanalysis. Our work demonstrates that the delignified bamboo can serve as a readily available support for enzyme immobilization and hierarchical bioreactor construction, which will potentially increase the robustness of enzymes in analytical and synthetical applications.

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Section: Results and Discussionmentioning

confidence: 95%

“…Comparison of immobilized efficiency versus specific surface area of different cellulose-based systems. − BSA (MW: 66.5 kDa) was used for the measurement in this work.…”

Section: Results and Discussionmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Enzyme Immobilization on a Delignified Bamboo Scaffold as a Green Hierarchical Bioreactor

Ren

Zhang

Sun

et al. 2022

ACS Sustainable Chem. Eng.

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“…More recently, CBM-assisted immobilization was reported for ωtransaminase from B. megaterium using the CBM CcCBM2a from Clostridium ellulovorans. 85,86 Enzyme Colocalization. Colocalization of enzymes in close proximity can confer a substantial advantage to enzymes that operate together either as part of a cascade or to provide cofactor recycling by relieving diffusional constraints on the reaction rate and increasing local substrate concentrations.…”

Section: Supramolecular Organization As a Tool For Continuous Flow Bi...mentioning

confidence: 99%

“…More recently, CBM-assisted immobilization was reported for ω-transaminase from B. megaterium using the CBM CcCBM2a from Clostridium ellulovorans. , …”

Section: Supramolecular Organization As a Tool For Continuous Flow Bi...mentioning

confidence: 99%

Engineering Enzyme Properties for Improved Biocatalytic Processes in Batch and Continuous Flow

Rocha

Speight

Scott

2022

Org. Process Res. Dev.

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The widespread adoption of biocatalysis by industry to perform highly selective chemical syntheses has been made possible only by the development of highly effective methods in enzyme engineering to overcome the limitations of naturally occurring enzymes. Through these methods we can adapt a broad range of enzyme properties, including interactions between enzymes and their substrates and cofactors and robustness of enzymes toward the nonphysiological environments of industrial processes, and even introduce new to nature chemical reactivities. The trend toward increased reaction complexity through the deployment of multienzyme cascades has also encouraged the development of engineering methods and design principles to improve cascade performance and accelerate their development, including engineering of spatial and temporal compartmentalization of cascades via biocatalyst colocation and immobilization. As the trend toward building reaction complexity continues, it is becoming clear that reaction design and engineering can be accelerated by the adoption of integrated multiscale engineering methods that are built around the concepts of standardization, modularity, and abstraction.

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Engineering of Covalent Organic Framework‐Based Advanced Platforms for Enzyme Immobilization: Strategies, Research Progress, and Prospects

Wang

Xia

Chen

2022

Adv Materials Inter

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Driven by green and sustainable methodologies for chemical manufacturing, enzymes are forecast to have much to prospect in the coming years due to their high activity and selectivity. However, the fragile active spatial‐conformation of an enzyme is predominantly maintained by weak intermolecular interactions, showing quite sensitive to thermal, pH, and chemical chemoreception. Thus, the low activity and recyclability result from structural instability can hardly meet the prototype of green chemistry in commercial process. Covalent organic frameworks (COFs) are stable extended porous network materials assembled by organic linkers in a moderate way. Due to their pre‐designable structures, an enzyme possesses the access to be immobilized to the interior or surface of COF skeletons via covalent or noncovalent processes, which can afford protection to enzymes in harsh conditions. Moreover, with the improved stability and cyclicity, the formed COF/enzyme biocomposites can facilitate broader horizon. Herein, this review mainly canvasses the advances in the emerging field of COF/enzyme biocomposites, sketching the factors that are critical in building COF/enzyme systems and the applications of registered enzyme host platforms reported in recent years.

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Enzyme immobilisation on wood-derived cellulose scaffolds via carbohydrate-binding module fusion constructs

Abstract: Enzyme-CBM fusion constructs immobilised on wood-derived cellulose scaffolds: a sustainable approach for continuous flow biocatalysis.

Cited by 21 publications

References 53 publications

Enzyme Immobilization on a Delignified Bamboo Scaffold as a Green Hierarchical Bioreactor

Enzyme Immobilization on a Delignified Bamboo Scaffold as a Green Hierarchical Bioreactor

Engineering Enzyme Properties for Improved Biocatalytic Processes in Batch and Continuous Flow

Engineering of Covalent Organic Framework‐Based Advanced Platforms for Enzyme Immobilization: Strategies, Research Progress, and Prospects

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