Co-immobilized carrier-free enzymes for lactose upgrading

Wilson, Lorena; Illanes, Andrés; Ottone, Carminna; Romero, Óscar

doi:10.1016/j.cogsc.2021.100553

Cited by 12 publications

(7 citation statements)

References 99 publications

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“…Numerous literature reviews have reported on a broad range of enzyme carriers [70]. The matrix for this enzyme immobilisation must have properties such as a high surface area, high permeability, higher degree of strength, high porosity, high chemical and thermal stability, resistance and inertness towards microbial attack, insolubility in water, easy synthesis, cost-effectiveness, and being green [71][72][73][74][75]. The matrices or supports for this novel technology can be categorised into the following: organic and inorganic compounds.…”

Section: Overview Of the Enzyme Carriers Materialsmentioning

confidence: 99%

Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

Mohidem,

Mohamad,

Rashid

et al. 2023

J. Compos. Sci.

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For over a century, enzyme immobilisation has been proven to be a superior strategy to improve catalytic activity and reusability and ensure easy separation, easy operation, and reduced cost. Enzyme immobilisation allows for an easier separation of the enzyme from the reaction mixture, thus simplifying downstream processing. This technology protects the enzyme from degradation or inactivation by harsh reaction conditions, making it more robust and suitable to be used in various applications. Recent strategies of immobilisation methods, such as adsorption, cross-linking, entrapment or encapsulation, and covalent bonding, were critically reviewed. These strategies have shown promising results in improving enzyme stability, activity, and reusability in various applications. A recent development in enzyme immobilisation in nanomaterials and agrowaste renewable carriers is underlined in the current review. Furthermore, the use of nanomaterials and agrowaste carriers in enzyme immobilisation has gained significant attention due to their unique properties, such as high surface area, high mass transfer, biocompatibility, and sustainability. These materials offer promising outcomes for developing more efficient and sustainable immobilised enzymes. This state-of-the-art strategy allows for better control over enzyme reactions and enhances their reusability, leading to more cost-effective and environmentally friendly processes. The use of renewable materials also helps to reduce waste generation and promote the utilisation of renewable resources, further contributing to the development of a circular economy.

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Section: Overview Of the Enzyme Carriers Materialsmentioning

confidence: 99%

Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

Mohidem,

Mohamad,

Rashid

et al. 2023

J. Compos. Sci.

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“…Although other alternatives to compensate the enzyme inactivation have been discussed in the literature, such as the addition of fresh enzyme, the increase of the reactor temperature [45,46] and the increase of the residence time in continuous reactor [19], none of them are compatible with the presented case of study. Moreover, the proposed catalyst replacement policy can be applied to other multi-enzyme systems where the enzymes involved might have quite different stabilities [17].…”

Section: Effect Of Modulation Of β-Gal Stability On the Production Of...mentioning

confidence: 99%

“…Catalysts 2021, 11, x FOR PEER REVIEW 2 of 15 profiles of the enzymes can differ significantly, as well as their operational stability [5,14,16]. Therefore, compromised operation conditions should be established to optimally balance their activity and operational stability [14,17], which is a key determinant of reactor performance [18,19].…”

Section: Introductionmentioning

confidence: 99%

Catalyst Replacement Policy on Multienzymatic Systems: Theoretical Study in the One-Pot Sequential Batch Production of Lactofructose Syrup

et al. 2021

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One-pot systems are an interesting proposal to carry out multi-enzymatic reactions, though this strategy implies establishing an optimal balance between the activity and operability of the involved enzymes. This is crucial for enzymes with marked differences in their operational stability, such as one-pot production of lactofructose syrup from cheese whey permeate, which involves two enzymes—β-galactosidase (β-gal) and glucose isomerase (GI). The aim of this work was to study the behavior of one-pot sequential batch production of lactofructose syrup considering both enzymes immobilized individually, in order to evaluate and design a strategy of replacement of the catalysts according to their stabilities. To this end, the modelling and simulation of the process was carried out, considering simultaneously the kinetics of both reactions and the kinetics of inactivation of both enzymes. For the latter, it was also considered the modulating effect that sugars present in the medium may have on the stability of β-gal, which is the less stable enzyme. At the simulated reaction conditions of 40 °C, pH 7, and 0.46 (IUGI/IUβ-gal), the results showed that considering the stability of b-gal under non-reactive conditions, meaning in absence of the effect of modulation, it is necessary to carry out four replacements of β-gal for each cycle of use of GI. On the other hand, when considering the modulation caused by the sugars on the b-gal stability, the productivity increases up to 23% in the case of the highest modulation factor studied (η = 0.8). This work shows the feasibility of conducting a one-pot operation with immobilized enzymes of quite different operational stability, and that a proper strategy of biocatalyst replacement increases the productivity of the process.

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“…CLEA has been successfully employed for a vast diversity of biotechnological applications, from preparing pharmaceuticals (as sem-synthetic penicillins and cephalosporins), nutraceuticals, cosmetic ingredients, etc carbohydrate conversion processes, among others ( Sheldon et al, 2013 ; Sheldon, 2019 ). More recently, CLEAs have been applied in the biomass conversion, aimed at valorizing food by-products, where feruloyl esterase CLEAs have been successfully employed to obtain high-valued bioactive compounds as phenolic acids from cereals and grains wastes ( Grajales-Hernández et al, 2021 ); and to revalorize dairy by-products producing lactofructose syrup from whey surplus ( Wilson et al, 2022 ). Additionally, the CLEA approach has enabled the stabilization of complex multi-domain enzymes whose applications at large-scale preparation processes are hampered by their low stability in vitro conditions ( Wagner et al, 2021 ).…”

mentioning

confidence: 99%

“…Furthermore, multi-task robust aggregates can be prepared by co-precipitation and cross-linking of two or more enzymes in “combined CLEAs” (combi-CLEA). These can catalyze multiple cascade reactions with different potential applications; as to simplify multi-step processes in one-pot (as the combi-CLEA of β-Galactosidase and glucose isomerase synthesizing lacto-fructose syrup ( Wilson et al, 2022 )); for the efficient cofactor regeneration (as the combi-CLEA formed by glycerol dehydrogenase and NADH oxidase ( Xu et al, 2020 ) and the combi-CLEA of BVMO and FDH for the synthesis of S -omeprazole); and the hydrolysis of complex molecules requiring more than one enzymatic activity (as the combi-CLEA of xylanase and mannanase employed in the hydrolysis of lignocellulose waste for the production of second generation of biodiesel ( Bhattacharya and Pletschke, 2015 )); among others.…”

mentioning

confidence: 99%

Editorial: Designing Carrier-Free Immobilized Enzymes for Biocatalysis

Velasco‐Lozano

Rocha-Martín

Santos

2022

Front. Bioeng. Biotechnol.

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Editorial on the Research TopicDesigning Carrier-free Immobilized Enzymes for Biocatalysis Global challenges in energy, resources, environment and sustainable chemical processing are leading us to minimize the use of natural resources, toxic materials, energy, and the generation of waste and pollutants. Enzymatic biocatalysis development evolves to strengthen the ongoing required process improvements of current industrial chemical transformations, where enzymes are naturally available, efficient biocatalysts exhibiting high specificity and enantioselectivity. However, for their industrial application, enzymes must possess high stability under large-scale producing conditions (such as high substrate and product concentrations, temperature, presence of solvents), where enzymes easily become inactive due to their low stability under such unnatural conditions or the almost null activity toward non-natural substrates. In this context, enzyme immobilization is a strategy that can facilitate their stabilization, purification, and reuse in the industry (Cavalcante et al., 2021; da S. Moreira et al., 2021;Reis et al., 2019). Enzymes can be immobilized on water-insoluble supports or without supports. Among carrier-free immobilization methods, the Cross-Linked Enzyme Aggregates (CLEA) emerged as a promising technology capable of manufacturing robust immobilized protein aggregates. In general, the preparation of CLEA involves the first stage of precipitation of enzymatic molecules followed by a cross-linking step managed by the action of a bifunctional reagent added to the reaction system, the cross-linker. As a result, the aggregates become insoluble, maintaining high catalytic activity, excellent stability, and low production cost.Another possibility of immobilizing enzymes free of support is the cross-linked enzyme crystals (CLEC). Compared to soluble enzymes, CLEC is more robust, controllable in size, resistant to organic solvents, and inactivates by heat or proteolysis. However, in contrast with CLEA, CLEC requires purified enzymes to achieve the required enzyme crystals formation, thus hampering their implementation at significant scale processes.CLEAs's physical and catalytic properties are strongly influenced and controlled through the preparation process (Table 1). Several works have summarized the most reported variables leading to robust CLEA biocatalysts from a wide variety of different enzymes, such as hydrolases, oxidoreductases, lyases, transferases, and isomerases for different industrial applications (Talekar

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Co-immobilized carrier-free enzymes for lactose upgrading

Cited by 12 publications

References 99 publications

Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

Recent Advances in Enzyme Immobilisation Strategies: An Overview of Techniques and Composite Carriers

Catalyst Replacement Policy on Multienzymatic Systems: Theoretical Study in the One-Pot Sequential Batch Production of Lactofructose Syrup

Editorial: Designing Carrier-Free Immobilized Enzymes for Biocatalysis

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