Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

Tacias-Pascacio, Veymar G.; Ortíz, Claudia; Rueda, Nazzoly; Berenguer-Murcia, Ángel; Acosta, Niuris; Aranaz, Inmaculada; Tejuca, María Concepción Civera; Fernández-Lafuente, Roberto; León, Andrés Rafael Alcántara

doi:10.3390/catal9070622

Cited by 40 publications

(28 citation statements)

References 315 publications

(383 reference statements)

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“…The use of PEI-coated carriers ensures strong ionic interaction with the enzyme, avoiding the limitations typical of covalent immobilization [ 41 ]. Similarly, the use of dextran aldehyde allows the stabilization of enzyme-carrier interactions by crosslinking, preventing the dissociation of enzymatic subunits [ 59 ].…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Bodakowska-Boczniewicz

Garncarek

2020

Molecules

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Naringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize naringinase from Aspergillus niger KMS on a magnetic carrier obtained on the basis of carob gum activated by polyethyleneimine. Response surface methodology was used to optimize naringinase immobilization taking into account the following factors: pH, immobilization time, initial concentration of naringinase and immobilization temperature. The adsorption of the enzyme on a magnetic carrier was a reversible process. The binding force of naringinase was increased by crosslinking the enzyme with the carrier using dextran aldehyde. The crosslinked enzyme had better stability in an acidic environment and at a higher temperature compared to the free form. The immobilization and stabilization of naringinase by dextran aldehyde on the magnetic polysaccharide carrier lowered the activation energy, thus increasing the catalytic capacity of the investigated enzyme and increasing the activation energy of the thermal deactivation process, which confirms higher stability of the immobilized enzyme in comparison with free naringinase. The preparation of crosslinked naringinase retained over 80% of its initial activity after 10 runs of naringin hydrolysis from fresh and model grapefruit juice.

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Section: Resultsmentioning

confidence: 99%

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Bodakowska-Boczniewicz

Garncarek

2020

Molecules

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“…If the intermolecular crosslinking is properly developed to include most of the enzymes in the PCMC, this could give a kind of "empty globe" formed by crosslinked enzyme molecules, which could find many different applications. This massive inter-protein crosslinked may be achieved using dextran aldehyde instead of glutaraldehyde [182], and fully protein loaded PCMC to make easier this crosslinking.…”

Section: Discussionmentioning

confidence: 99%

“…The authors observed that just the stirring of the enzymes in the reaction medium promoted an inactivation, which was attributed to the action of shearing force on the enzyme molecules because the enzyme is located on the support surface [175]. This problem is general for any nanomaterial where the enzyme is located on the surface [181] and could be at least partially solved if coating the enzyme molecules with some polymers [181][182][183][184][185].…”

Section: Chemically Crosslinked Pcmcsmentioning

confidence: 99%

Enzyme-Coated Micro-Crystals: An Almost Forgotten but Very Simple and Elegant Immobilization Strategy

et al. 2020

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The immobilization of enzymes using protein coated micro-crystals (PCMCs) was reported for the first time in 2001 by Kreiner and coworkers. The strategy is very simple. First, an enzyme solution must be prepared in a concentrated solution of one compound (salt, sugar, amino acid) very soluble in water and poorly soluble in a water-soluble solvent. Then, the enzyme solution is added dropwise to the water soluble solvent under rapid stirring. The components accompanying the enzyme are called the crystal growing agents, the solvent being the dehydrating agent. This strategy permits the rapid dehydration of the enzyme solution drops, resulting in a crystallization of the crystal formation agent, and the enzyme is deposited on this crystal surface. The reaction medium where these biocatalysts can be used is marked by the solubility of the PCMC components, and usually these biocatalysts may be employed in water soluble organic solvents with a maximum of 20% water. The evolution of these PCMC was to chemically crosslink them and further improve their stabilities. Moreover, the PCMC strategy has been used to coimmobilize enzymes or enzymes and cofactors. The immobilization may permit the use of buffers as crystal growth agents, enabling control of the reaction pH in the enzyme environments. Usually, the PCMC biocatalysts are very stable and more active than other biocatalysts of the same enzyme. However, this simple (at least at laboratory scale) immobilization strategy is underutilized even when the publications using it systematically presented a better performance of them in organic solvents than that of many other immobilized biocatalysts. In fact, many possibilities and studies using this technique are lacking. This review tried to outline the possibilities of this useful immobilization strategy.

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“…All the enzymes were used as immobilized biocatalysts according to our previous investigations. Thus, CpUP and AhPNP were used upon covalent immobilization on glyoxyl-agarose [18], whereas DddAK was immobilized by a ionic interaction on an epoxy carrier (Sepabeads ® EC-EP) previously coated with polyethylenimine (PEI), followed by cross-linking with a polyaldehyde (CL) [12,27]. In agreement also with recent reports [25,26], this latter approach results in a sort of "co-immobilization" of the co-factor (ATP, in this case), thus ensuring a self-sufficient source of it for an efficient catalysis.…”

Section: A Three-enzyme Cascade For the Synthesis Of Araa-mpmentioning

confidence: 99%

A Multi-Enzymatic Cascade Reaction for the Synthesis of Vidarabine 5′-Monophosphate

et al. 2020

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We here described a three-step multi-enzymatic reaction for the one-pot synthesis of vidarabine 5′-monophosphate (araA-MP), an antiviral drug, using arabinosyluracil (araU), adenine (Ade), and adenosine triphosphate (ATP) as precursors. To this aim, three enzymes involved in the biosynthesis of nucleosides and nucleotides were used in a cascade mode after immobilization: uridine phosphorylase from Clostridium perfringens (CpUP), a purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP), and deoxyadenosine kinase from Dictyostelium discoideum (DddAK). Specifically, CpUP catalyzes the phosphorolysis of araU thus generating uracil and α-d-arabinose-1-phosphate. AhPNP catalyzes the coupling between this latter compound and Ade to form araA (vidarabine). This nucleoside becomes the substrate of DddAK, which produces the 5′-mononucleotide counterpart (araA-MP) using ATP as the phosphate donor. Reaction conditions (i.e., medium, temperature, immobilization carriers) and biocatalyst stability have been balanced to achieve the highest conversion of vidarabine 5′-monophosphate (≥95.5%). The combination of the nucleoside phosphorylases twosome with deoxyadenosine kinase in a one-pot cascade allowed (i) a complete shift in the equilibrium-controlled synthesis of the nucleoside towards the product formation; and (ii) to overcome the solubility constraints of araA in aqueous medium, thus providing a new route to the highly productive synthesis of araA-MP.

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Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

Cited by 40 publications

References 315 publications

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Enzyme-Coated Micro-Crystals: An Almost Forgotten but Very Simple and Elegant Immobilization Strategy

A Multi-Enzymatic Cascade Reaction for the Synthesis of Vidarabine 5′-Monophosphate

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