Synthesis and characterization of magnetic cross-linked enzyme aggregate and its evaluation of the alternating magnetic field (AMF) effects in the catalytic activity

Lucena, Guilherme Nunes; Santos, Caio Carvalho dos; Pinto, Gabriel Cardoso; Piazza, Rodolfo Debone; Guedes, Wesley Nascimento; Júnior, Miguel Jafelicci; Paula, Ariela Veloso de; Marques, Rodrigo Fernando Costa

doi:10.1016/j.jmmm.2020.167326

Cited by 13 publications

(8 citation statements)

References 43 publications

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“…The same as for CLEAs plus eased recovery of the biocatalyst using a magnetic field Same as for CLEAs but cluster/clump formation avoided since recovery circumvents filtration/centrifugation [25,[105][106][107][108] Enzyme cross-linking upon adsorption to minimize leakage.…”

Section: Classification Of Immobilization Methods and Their Key Featuresmentioning

confidence: 99%

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

et al. 2022

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Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability.

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Section: Classification Of Immobilization Methods and Their Key Featuresmentioning

confidence: 99%

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

et al. 2022

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“…Alteration of the enzyme tertiary structure by one of the components required for CLEA preparation or steric hindrance within the aggregate of high particle size hampering inner A wide variety of enzymes, including hydrolases, oxidoreductases, lyases, and transferases have been used as CLEAs especially for organic synthesis [172,173], displaying enhanced stability under various conditions: protection against organic solvents [174], enhanced thermostability [175], reduced substrate inhibition [176,177], enhanced stability in acidic or alkaline conditions [178,179] or under storage [180]. Magnetic CLEAs combined the advantages of CLEAs and covalent immobilization onto Fe 3 O 4 magnetic particles and may show increased stability to changes of pH and temperature [181,182]. Enzyme cascade can also be combined as CLEAs showing enhanced thermal and pH stability [183,184].…”

Section: Cross-linked Enzyme Aggregates (Cleas)mentioning

confidence: 99%

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

et al. 2021

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Bioelectrocatalysis using redox enzymes appears as a sustainable way for biosensing, electricity production, or biosynthesis of fine products. Despite advances in the knowledge of parameters that drive the efficiency of enzymatic electrocatalysis, the weak stability of bioelectrodes prevents large scale development of bioelectrocatalysis. In this review, starting from the understanding of the parameters that drive protein instability, we will discuss the main strategies available to improve all enzyme stability, including use of chemicals, protein engineering and immobilization. Considering in a second step the additional requirements for use of redox enzymes, we will evaluate how far these general strategies can be applied to bioelectrocatalysis.

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“…Magnetic field treatment can enhance microbial metabolic pathways leading to the accumulation of carbohydrates, thus stimulating growth [140] . Magnetic field treatment can interfere with enzyme kinetics and alter enzyme activity by increasing the rate of collision between biocatalysts and substrates, by altering the aggregation state of enzymes, by triggering conformational changes in enzymes, or by increasing the rate of diffusion [141] .…”

Section: Physical Field Technology Characteristics and Mechanisms Of Actionmentioning

confidence: 99%

Prospects and application of ultrasound and magnetic fields in the fermentation of rare edible fungi

Wen

et al. 2021

Ultrasonics Sonochemistry

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Synthesis and characterization of magnetic cross-linked enzyme aggregate and its evaluation of the alternating magnetic field (AMF) effects in the catalytic activity

Cited by 13 publications

References 43 publications

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

Prospects and application of ultrasound and magnetic fields in the fermentation of rare edible fungi

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