Hybrid chemoenzymatic heterogeneous catalyst prepared in one step from zeolite nanocrystals and enzyme–polyelectrolyte complexes

Verren, Margot Van der; Smeets, Valentin; Straeten, Aurélien vander; Dupont-Gillain, Christine; Debecker, Damien P.

doi:10.1039/d0na00834f

Cited by 17 publications

(8 citation statements)

References 90 publications

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“…The enhanced local enzyme concentration inside the PNCs may result in a higher kinetic efficiency than would occur with the same concentration of the enzyme dispersed in solution. Such a local environment is sometimes exploited to boost enzyme stability in the case of enzyme−polyelectrolyte complexes 30 or to tune the local pH. 31 In addition, both free and co-encapsulated systems showed a similar trend in D-mannitol production (Figure S5).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Nano-Entrapping Multiple Oxidoreductases and Cofactor for All-In-One Nanoreactors

Kim

Kwon

Tae

et al. 2021

ACS Sustainable Chem. Eng.

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Oxidoreductases have been used for the synthesis of value-added chemicals via redox reactions under mild conditions. However, these enzymes often require cofactors, which are expensive and small molecules making them difficult to reuse in the popular immobilized enzyme processes. Here, we show that nicotinamide adenine dinucleotide-conjugated alginate (AlgNAD + ) can overcome these cofactor limitations after in situ co-encapsulation with two oxidoreductases, formate dehydrogenase (FDH), and mannitol dehydrogenase (MDH), inside pluronic-based nanocarriers (PNCs). PNCs had high encapsulation yields for FDH and MDH (both >80%) and AlgNAD + (46.5%). AlgNAD + -co-encapsulated enzymes displayed enhanced catalytic activity compared with the free enzymes. Furthermore, we could control the amount of the encapsulated AlgNAD + in the PNC by varying its input, thereby enabling efficient construction of a cofactor regeneration system. Moreover, PNC-co-encapsulated FDH, MDH, and AlgNAD + produced triplicate batches of D-mannitol after separating the reaction products from the co-encapsulated complex, with no cofactor supplementation. These results demonstrate that PNC can efficiently co-encapsulate enzymes and cofactors in the desired amounts generating All-in-One nanoreactors for repeated enzymatic reactions.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Nano-Entrapping Multiple Oxidoreductases and Cofactor for All-In-One Nanoreactors

Kim

Kwon

Tae

et al. 2021

ACS Sustainable Chem. Eng.

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“…This is a rare feature of other enzyme immobilization methods, [30b] as in most cases the enzymes are covalently bonded to the support material and are therefore difficult to detach. [32,34] Two related methods are i) the "layer-by-layer" (LbL) deposition method, [52] with which charged polymers (polyelectrolytes) and oppositely charged enzymes are deposited on (silica) surfaces by simple adsorption, and ii) the "enzyme-polyelectrolyte complexes" (EPC) method, [53] in which oppositely charged polyelectrolytes are wrapped around the enzyme to be adsorbed, or a combination of LbL and EPC. [54] Obviously, the LBL and EPC methods do not involve the covalent attachment of enzymes to polymer molecules.…”

Section: Discussionmentioning

confidence: 99%

Performance of a Flow‐Through Enzyme Reactor Prepared from a Silica Monolith and an α‐Poly(D‐Lysine)‐Enzyme Conjugate

Ghéczy

Tao

Pour-Esmaeil

et al. 2023

Macromolecular Bioscience

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Horseradish peroxidase (HRP) is covalently bound in aqueous solution to polycationic α‐poly(D‐lysine) chains of ≈1000 repeating units length, PDL, via a bis‐aryl hydrazone bond (BAH). Under the experimental conditions used, about 15 HRP molecules are bound along the PDL chain. The purified PDL‐BAH‐HRP conjugate is very stable when stored at micromolar HRP concentration in a pH 7.2 phosphate buffer solution at 4 °C. When a defined volume of such a conjugate solution of desired HRP concentration (i.e., HRP activity) is added to a macro‐ and mesoporous silica monolith with pore sizes of 20–30 µm as well as below 30 nm, quantitative and stable noncovalent conjugate immobilization is achieved. The HRP‐containing monolith can be used as flow‐through enzyme reactor for bioanalytical applications at neutral or slightly alkaline pH, as demonstrated for the determination of hydrogen peroxide in diluted honey. The conjugate can be detached from the monolith by simple enzyme reactor washing with an aqueous solution of pH 5.0, enabling reloading with fresh conjugate solution at pH 7.2. Compared to previously investigated polycationic dendronized polymer‐enzyme conjugates with approximately the same average polymer chain length, the PDL‐BAH‐HRP conjugate appears to be equally suitable for HRP immobilization on silica surfaces.

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“…cross-linking of entrapped enzymes to prevent their leaching from the carrier porosity). 154,162,163…”

Section: Transaminase-catalysed Synthesis Of Amines: Industrial Relev...mentioning

confidence: 99%

Continuous flow-mode synthesis of (chiral) amines with transaminase: a strategic biocatalytic approach to essential building blocks

et al. 2023

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Hybrid chemoenzymatic heterogeneous catalyst prepared in one step from zeolite nanocrystals and enzyme–polyelectrolyte complexes

Abstract: A suspension of TS-1 zeolite nanocrystals and glucose oxidase–polyelectrolyte complexes is spray-dried to form, in one step, a hybrid chemo-enzymatic heterogeneous catalyst utilized for the production of H2O2 cascaded with allyl alcohol epoxidation.

Cited by 17 publications

References 90 publications

Nano-Entrapping Multiple Oxidoreductases and Cofactor for All-In-One Nanoreactors

Nano-Entrapping Multiple Oxidoreductases and Cofactor for All-In-One Nanoreactors

Performance of a Flow‐Through Enzyme Reactor Prepared from a Silica Monolith and an α‐Poly(D‐Lysine)‐Enzyme Conjugate

Continuous flow-mode synthesis of (chiral) amines with transaminase: a strategic biocatalytic approach to essential building blocks

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