Co-immobilization of multiple enzymes onto surface-functionalized magnetic nanoparticle for the simultaneous hydrolysis of multiple substrates containing industrial wastes

Suganthi, S.; Swathi, K.; Biswas, Raagini; Basker, Sneha; Ramani, K.

doi:10.1007/s13204-019-01125-y

Cited by 15 publications

(11 citation statements)

References 38 publications

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“…Co-immobilization (MNP-PEA-OmpA-Laccase) led to a second weight loss of 5.6%, which shows a subtle improvement in efficiency. This could be attributed to the interplay and competition of protein-protein and protein-surface interactions during immobilization [ 69 , 70 , 71 , 72 ]. Further studies will be required to maximize the efficiencies.…”

Section: Resultsmentioning

confidence: 99%

“…The enzyme contents were estimated based on the enzymatic activity as described in Supplementary Materials, Section SI5 and Figure S4 . This approach followed previous reports where the number of active immobilized molecules has been estimated by quantifying their catalytic activity towards a substrate with the aid of colorimetric or fluorescent methods [ 69 , 74 , 75 , 76 ]. Figure 3 c shows the immobilization yield obtained according to content of Laccase.…”

Section: Resultsmentioning

confidence: 99%

“…Several other materials have been coated on the surface of MNP to improve their porosity, stability, or affinity for specific interfaces [ 77 ]. Examples of them include APTES [ 40 ], polymers [ 14 , 41 ], carbon structures [ 15 , 38 , 39 ], and enzymes [ 69 , 78 ]. The process of co-immobilization is intended to not only take advantage of the properties of MNPs, but also the properties of the interfaced molecules either independently or synergistically.…”

Section: Resultsmentioning

confidence: 99%

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Novel Bionanocompounds: Outer Membrane Protein A and Laccase Co-Immobilized on Magnetite Nanoparticles for Produced Water Treatment

et al. 2020

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The oil and gas industry generates large amounts of oil-derived effluents such as Heavy Crude Oil (HCO) in water (W) emulsions, which pose a significant remediation and recovery challenge due to their high stability and the presence of environmentally concerning compounds. Nanomaterials emerge as a suitable alternative for the recovery of such effluents, as they can separate them under mild conditions. Additionally, different biomolecules with bioremediation and interfacial capabilities have been explored to functionalize such nanomaterials to improve their performance even further. Here, we put forward the notion of combining these technologies for the simultaneous separation and treatment of O/W effluent emulsions by a novel co-immobilization approach where both OmpA (a biosurfactant) and Laccase (a remediation enzyme) were effectively immobilized on polyether amine (PEA)-modified magnetite nanoparticles (MNPs). The obtained bionanocompounds (i.e., MNP-PEA-OmpA, MNP-PEA-Laccase, and MNP-PEA-OmpA-Laccase) were successfully characterized via DLS, XRD, TEM, TGA, and FTIR. The demulsification of O/W emulsions was achieved by MNP-PEA-OmpA and MNP-PEA-OmpA-Laccase at 5000 ppm. This effect was further improved by applying an external magnetic field to approach HCO removal efficiencies of 81% and 88%, respectively. The degradation efficiencies with these two bionanocompounds reached levels of between 5% and 50% for the present compounds. Taken together, our results indicate that the developed nanoplatform holds significant promise for the efficient treatment of emulsified effluents from the oil and gas industry.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Novel Bionanocompounds: Outer Membrane Protein A and Laccase Co-Immobilized on Magnetite Nanoparticles for Produced Water Treatment

et al. 2020

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“…One of the points is that coimmobilization is only reasonable when that has some clear advantage over individual enzyme immobilization, e.g., in cascade reactions [60,287] (Figures 22-25). However, in some instances, the problems are ignored and several enzymes are coimmobilized, even stating that the intention is not to produce a biocatalyst to catalyze cascade reactions in one pot, but to produce the so-called "multipurpose biocatalysts" [32,451]. This is the case of the preparation of a combiCLEA containing lipase, α-amylase, and phospholipase A2 [452].…”

Section: Preparation Of Coimmobilized Combilipases To Reuse the Most Stable Enzymesmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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“…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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Co-immobilization of multiple enzymes onto surface-functionalized magnetic nanoparticle for the simultaneous hydrolysis of multiple substrates containing industrial wastes

Cited by 15 publications

References 38 publications

Novel Bionanocompounds: Outer Membrane Protein A and Laccase Co-Immobilized on Magnetite Nanoparticles for Produced Water Treatment

Novel Bionanocompounds: Outer Membrane Protein A and Laccase Co-Immobilized on Magnetite Nanoparticles for Produced Water Treatment

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

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

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