Enzyme co-immobilization: Always the biocatalyst designers' choice…or not?

Arana-Peña, Sara; Carballares, Diego; Morellon-Sterlling, Roberto; Berenguer-Murcia, Ángel; Alcántara, Andrés R.; Rodrigues, Rafael C.; Fernández-Lafuente, Roberto

doi:10.1016/j.biotechadv.2020.107584

Cited by 190 publications

(224 citation statements)

References 324 publications

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“…[215][216][217][218][219][220][221] However, co-immobilization, that is, the immobilization of two or more enzymes on the same particle, has advantages but also has some serious drawbacks that in many instances are not taken into account. 222 Among the clearest advantages, we can note the shortening of the induction time for the second enzyme to act, which increases the initial rate of the global process 105,106 (Fig. 8).…”

Section: Use Of Catalases and Glucose Oxidase To Produce D-gluconic Amentioning

confidence: 99%

Enzyme production ofd-gluconic acid and glucose oxidase: successful tales of cascade reactions

Kornecki

Carballares

Tardioli

et al. 2020

Catal. Sci. Technol.

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115

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Section: Use Of Catalases and Glucose Oxidase To Produce D-gluconic Amentioning

confidence: 99%

Enzyme production ofd-gluconic acid and glucose oxidase: successful tales of cascade reactions

Kornecki

Carballares

Tardioli

et al. 2020

Catal. Sci. Technol.

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115

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“…However, in some instances, this is a requirement not related to the shortening of the reaction course, but with the final yields, e.g., when some of the intermediate products are not stable and can lead to another compound different from the target, producing a decrease in the reaction yield and a complication on the final purification of the target compound, as contaminant compounds will appear in the final reaction medium [35,44]. However, as recently reviewed, co-immobilization presents many problems (e.g., necessity of using the same support surface, different stability of the coimmobilized enzymes) [190,191], and the researcher must analyzed if the co-immobilization problems compensate the advantages (for a revision of this topic, consult [192].…”

Section: Enzyme Co-immobilizationmentioning

confidence: 99%

“…Moreover, also some coimmobilized biocatalysts of protease and lipases were prepared, for non-cascade reactions [193]. These biocatalysts, called multipurpose biocatalyst [195][196][197], have unclear advantages and many disadvantages [192].…”

Section: Enzyme Co-immobilizationmentioning

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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“…Lipases co-immobilization raised some kinetic advantages in cascade reactions, as all the enzymes are exposed to high concentrations of the intermediate products from the first time of the reaction, eliminating the usual lag time in these processes [65,66]. However, conventional co-immobilization has some problems, like the fact that all enzymes must be immobilized on the same support surface using the same chemistry, and that, if the stabilities of the enzymes greatly differ under operational conditions, all immobilized enzymes must be discarded after the inactivation of the least stable enzyme even when the other enzymes maintain their full initial activities [65,67]. This seems just a technological problem, but it can prevent the industrial implementation of co-immobilized lipases.…”

Section: Introductionmentioning

confidence: 99%

“…This seems just a technological problem, but it can prevent the industrial implementation of co-immobilized lipases. Usually, different long term enzyme stability problem on the design of co-immobilized enzymes is ignored [65,67].…”

Section: Introductionmentioning

confidence: 99%

Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones

et al. 2020

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The lipases A and B from Candida antarctica (CALA and CALB), Thermomyces lanuginosus (TLL) or Rhizomucor miehei (RML), and the commercial and artificial phospholipase Lecitase ultra (LEU) may be co-immobilized on octyl agarose beads. However, LEU and RML became almost fully inactivated under conditions where CALA, CALB and TLL retained full activity. This means that, to have a five components co-immobilized combi-lipase, we should discard 3 fully active and immobilized enzymes when the other two enzymes are inactivated. To solve this situation, CALA, CALB and TLL have been co-immobilized on octyl-vinyl sulfone agarose beads, coated with polyethylenimine (PEI) and the least stable enzymes, RML and LEU have been co-immobilized over these immobilized enzymes. The coating with PEI is even favorable for the activity of the immobilized enzymes. It was checked that RML and LEU could be released from the enzyme-PEI coated biocatalyst, although this also produced some release of the PEI. That way, a protocol was developed to co-immobilize the five enzymes, in a way that the most stable could be reused after the inactivation of the least stable ones. After RML and LEU inactivation, the combi-biocatalysts were incubated in 0.5 M of ammonium sulfate to release the inactivated enzymes, incubated again with PEI and a new RML and LEU batch could be immobilized, maintaining the activity of the three most stable enzymes for at least five cycles of incubation at pH 7.0 and 60 °C for 3 h, incubation on ammonium sulfate, incubation in PEI and co-immobilization of new enzymes. The effect of the order of co-immobilization of the different enzymes on the co-immobilized biocatalyst activity was also investigated using different substrates, finding that when the most active enzyme versus one substrate was immobilized first (nearer to the surface of the particle), the activity was higher than when this enzyme was co-immobilized last (nearer to the particle core).

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Enzyme co-immobilization: Always the biocatalyst designers' choice…or not?

Cited by 190 publications

References 324 publications

Enzyme production ofd-gluconic acid and glucose oxidase: successful tales of cascade reactions

Enzyme production ofd-gluconic acid and glucose oxidase: successful tales of cascade reactions

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

Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones

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