Strategies to rationalize enzyme immobilization procedures

Sastre, Diego E.; Reis, Eduardo Arizono dos; Netto, Caterina Gruenwaldt Cunha Marques

doi:10.1016/bs.mie.2019.09.003

Cited by 28 publications

(17 citation statements)

References 90 publications

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“…Further, the efficiency and stability of purified free chitinases are generally less, which can be improved by immobilization [ 97 ]. Enzyme immobilization is used to achieve stable, reusable, and more active enzymes by the simple act of fixing an enzyme on a support surface [ 98 ]. Various types of supports are used for immobilization, and, amidst them, magnetic nanoparticles (MNPs) of 10 to 20 nm are highly favored, due to their non-toxicity, large surface area and surface: volume ratio, and the simplicity in separating the biocatalyst after use.…”

Section: Microbial Fermentation For Chitinase Productionmentioning

confidence: 99%

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Poria

Rana

Kumari

et al. 2021

Biology

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Chitinases are a large and diversified category of enzymes that break down chitin, the world’s second most prevalent polymer after cellulose. GH18 is the most studied family of chitinases, even though chitinolytic enzymes come from a variety of glycosyl hydrolase (GH) families. Most of the distinct GH families, as well as the unique structural and catalytic features of various chitinolytic enzymes, have been thoroughly explored to demonstrate their use in the development of tailor-made chitinases by protein engineering. Although chitin-degrading enzymes may be found in plants and other organisms, such as arthropods, mollusks, protozoans, and nematodes, microbial chitinases are a promising and sustainable option for industrial production. Despite this, the inducible nature, low titer, high production expenses, and susceptibility to severe environments are barriers to upscaling microbial chitinase production. The goal of this study is to address all of the elements that influence microbial fermentation for chitinase production, as well as the purifying procedures for attaining high-quality yield and purity.

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Section: Microbial Fermentation For Chitinase Productionmentioning

confidence: 99%

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Poria

Rana

Kumari

et al. 2021

Biology

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“…Strategies allowing for controlled reversibility of immobilization have also been described [44][45][46]. Lastly, different methodologies have been suggested towards a more rational approach for enzyme immobilization, which include: detailed knowledge of the physical and chemical properties of both enzyme and carrier (e.g., distribution of hydrophobic and hydrophilic regions in the carrier and hydrophobic and polar regions in the surface of individual enzyme; carrier porosity, including pore size distribution, structure and volume carrier chemical and mechanical endurance of operational conditions); generation of databases and use of bioinformatics and other computational tools for improved characterization of enzymes and corresponding catalytic features; factorial planning; and protein engineering to enable a specific enzyme orientation on a carrier [37,[47][48][49][50][51]. Overall, once optimized, enzyme immobilization is intended to provide a biocatalyst formulation that may lead to total turnover number (TTN), defined as the total moles of product produced per mole of enzyme over the entire lifetime of the enzyme, over either 10 3 (for expensive products produced at small scale) or 5 × 10 5 -5 × 10 6 (for low-cost products/commodities), according to the thresholds required in industry [52][53][54].…”

Section: Enzyme Immobilization: Drivers Limitations and Metricsmentioning

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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“…At the end of the experiment, the MN-POD had 13546 U mg -1 of speci c activity, corresponding to 5% of RA. Both activity and degradation e ciency decay are expected in reusability assays, considering that the enzyme active site and the support pore voids are lled over cycles 9,44 .…”

Section: Strategies For T Koningiopsis Peroxidase Immobilizationmentioning

confidence: 99%

Complete wastewater discoloration by a novel peroxidase source with promising bioxidative properties

Klanovicz

Stefanski

Camargo

et al. 2022

Preprint

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BACKGROUND Our study aimed to characterize and prospect immobilization strategies for a novel fungal peroxidase - POD (EC 1.11.1.7) and to insert it in the context of pollutant remediation, since these compounds pose risks to human and environmental health. The enzymatic extract was obtained by submerged fermentation of the fungus Trichoderma koningiopsis in an alternative substrate, consisting of fresh microalgal biomass. The immobilization efficiency was evaluated by monitoring the residual activity (RA) and the discoloration potential (DP) of a synthetic dye solution. Concomitantly, the catalytic properties of free POD were explored, and the most promising storage strategy to maintain the enzymatic activity was studied. RESULTS The novel guaiacol peroxidase expressed specific activity of up to 7801 U mg−1 in the free form, showing stability when subjected to up to 80°C in a pH range between 4.0-8.0. Furthermore, the bioproduct immobilized on magnetic nanoparticles expressed up to 689% RA and 100% DP. An increase in the RA of the enzyme, both in free and immobilized form, was also observed after storage for up to 8 months. The synthesized magnetic nanozymes showed good reusability, maintaining 13546 U mg−1 after ten cycles and removing 94% of color in a second batch. Toxicological evaluation with Allium cepa indicated that the enzymatic process of color removal with immobilized POD was essential to eliminate genotoxic effects. CONCLUSION T. koningiopsis peroxidase production and immobilization presented in our work are promising for the enzyme market and for the wastewater treatment technologies, considering its high bioxidative potential.

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Strategies to rationalize enzyme immobilization procedures

Cited by 28 publications

References 90 publications

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

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

Complete wastewater discoloration by a novel peroxidase source with promising bioxidative properties

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