Special Issue "Immobilization of Enzymes"

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: 30 June 2019

Special Issue Editors

Guest Editor
Dr. Immacolata Serra

University of Milano, Department of Food, Environmental and Nutritional Sciences (DeFENS), Milano, Italy
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Interests: biocatalysis, heterologous protein expression, enzyme immobilization, enzyme engineering, multi-enzymatic processes, acylases, ketoreductases, nucleoside phosphorylases, fermentations
Guest Editor
Prof. Daniela Ubiali

University of Pavia, Department of Drug Sciences, Pavia, Italy
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Interests: biocatalysis, enzyme immobilization, nucleoside phosphorylases, lipases, omega-transaminases, biorefinery, medicinal chemistry

Special Issue Information

Dear Colleagues,

Enzymes are extremely versatile and powerful catalysts used in several fields (fine chemicals, pharmaceuticals, food, plastics, cosmetics, biofuels); moreover, they often represent an environmentally friendly alternative to conventional chemical catalysts. However, the competitiveness of biocatalyzed processes with respect to the “conventional” chemical ones is often hampered by the poor long-term operational stability of the biocatalysts and their difficult recovery and re-use. These drawbacks can generally be overcome by enzyme immobilization that, by definition, produces “an enzyme confined in a defined region of space with retention of catalytic activity, increased stability and which can be used repeatedly and continuously”. Thus, it is not surprising that enzyme immobilization is frequently considered as a pre-requisite to the development of an enzyme as a biocatalyst for synthetic applications.

Many efforts have been devoted over the years to the development of various immobilization techniques and materials. Nevertheless, the optimal immobilization technique often needs to be tailored for each enzyme to fit both the peculiar enzyme features and the final process. Combining information derived from protein sequence, 3-D structure, reaction mechanism and process features with data on physical/chemical properties of the carrier is pivotal to develop ad hoc immobilization strategies.

For this Special Issue, we welcome contributions from all aspects of enzyme immobilization, may they be related to fundamental science or practical applications, that can be outlined by the following keywords:

  • Enzyme immobilization techniques
  • Enzyme co-immobilization for cascade reactions
  • Rational design of immobilization
  • Improved enzyme properties via immobilization
  • Novel supports for enzyme immobilization
  • Enzyme modification to improve immobilization on solid support
  • Biotransformations catalyzed by immobilized enzymes

Dr. Immacolata Serra
Prof. Daniela Ubiali
Guest Editors

Manuscript Submission Information

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Keywords

  • Enzyme immobilization techniques
  • Enzyme co-immobilization for cascade reactions
  • Rational design of immobilization
  • Improved enzyme properties via immobilization
  • Novel supports for enzyme immobilization
  • Enzyme modification to improve immobilization on solid support
  • Biotransformations catalyzed by immobilized enzymes

Published Papers (4 papers)

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Research

Open AccessArticle Immobilization of Arylmalonate Decarboxylase
Catalysts 2018, 8(12), 603; https://doi.org/10.3390/catal8120603
Received: 25 September 2018 / Revised: 16 November 2018 / Accepted: 27 November 2018 / Published: 2 December 2018
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Abstract
Arylmalonate decarboxylase (AMD) is a monomeric enzyme of only 26 kDa. A recombinant AMDase from Bordetella bronchiseptica was expressed in Escherichia coli and the enzyme was immobilized using different techniques: entrapment in polyvinyl alcohol (PVA) gel (LentiKats®), covalent binding onto magnetic
[...] Read more.
Arylmalonate decarboxylase (AMD) is a monomeric enzyme of only 26 kDa. A recombinant AMDase from Bordetella bronchiseptica was expressed in Escherichia coli and the enzyme was immobilized using different techniques: entrapment in polyvinyl alcohol (PVA) gel (LentiKats®), covalent binding onto magnetic microparticles (MMP, PERLOZA s.r.o., Lovosice, Czech Republic) and double-immobilization (MMP-LentiKats®) using the previous two methods. The double-immobilized AMDase was stable in 8 repeated biocatalytic reactions. This combined immobilization technique has the potential to be applied to different small proteins. Full article
(This article belongs to the Special Issue Immobilization of Enzymes)
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Open AccessArticle Rice Husk as an Inexpensive Renewable Immobilization Carrier for Biocatalysts Employed in the Food, Cosmetic and Polymer Sectors
Catalysts 2018, 8(10), 471; https://doi.org/10.3390/catal8100471
Received: 23 September 2018 / Revised: 12 October 2018 / Accepted: 16 October 2018 / Published: 19 October 2018
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Abstract
The high cost and environmental impact of fossil-based organic carriers represent a critical bottleneck to their use in large-scale industrial processes. The present study demonstrates the applicability of rice husk as inexpensive renewable carrier for the immobilization of enzymes applicable sectors where the
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The high cost and environmental impact of fossil-based organic carriers represent a critical bottleneck to their use in large-scale industrial processes. The present study demonstrates the applicability of rice husk as inexpensive renewable carrier for the immobilization of enzymes applicable sectors where the covalent anchorage of the protein is a pre-requisite for preventing protein contamination while assuring the recyclability. Rice husk was oxidized and then functionalized with a di-amino spacer. The morphological characterization shed light on the properties that affect the functionalization processes. Lipase B from Candida antarctica (CaLB) and two commercial asparaginases were immobilized covalently achieving higher immobilization yield than previously reported. All enzymes were immobilized also on commercial epoxy methacrylic resins and the CaLB immobilized on rice husk demonstrated a higher efficiency in the solvent-free polycondensation of dimethylitaconate. CaLB on rice husk appears particularly suitable for applications in highly viscous processes because of the unusual combination of its low density and remarkable mechanical robustness. In the case of the two asparaginases, the biocatalyst immobilized on rice husk performed in aqueous solution at least as efficiently as the enzyme immobilized on methacrylic resins, although the rice husk loaded a lower amount of protein. Full article
(This article belongs to the Special Issue Immobilization of Enzymes)
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Open AccessArticle Preparation of a Flower-Like Immobilized D-Psicose 3-Epimerase with Enhanced Catalytic Performance
Catalysts 2018, 8(10), 468; https://doi.org/10.3390/catal8100468
Received: 31 July 2018 / Revised: 12 October 2018 / Accepted: 17 October 2018 / Published: 18 October 2018
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Abstract
In this present study, we proposed a smart biomineralization method for creating hybrid organic–inorganic nanoflowers using a Co2+-dependent enzyme (D-psicose 3-epimerase; DPEase) as the organic component and cobalt phosphate as the inorganic component. The prepared nanoflowers have many separated
[...] Read more.
In this present study, we proposed a smart biomineralization method for creating hybrid organic–inorganic nanoflowers using a Co2+-dependent enzyme (D-psicose 3-epimerase; DPEase) as the organic component and cobalt phosphate as the inorganic component. The prepared nanoflowers have many separated petals that have a nanometer size. Under optimum conditions (60 °C and pH of 8.5), the nanoflower can display its maximum activity (36.2 U/mg), which is about 7.2-fold higher than free DPEase. Furthermore, the immobilized DPEase presents enhanced pH and thermal stabilities. The DPEase-nanoflower maintained about 90% of its activity after six reaction cycles, highlighting its excellent reusability. Full article
(This article belongs to the Special Issue Immobilization of Enzymes)
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Open AccessArticle Stabilization of Enzymes by Multipoint Covalent Attachment on Aldehyde-Supports: 2-Picoline Borane as an Alternative Reducing Agent
Catalysts 2018, 8(8), 333; https://doi.org/10.3390/catal8080333
Received: 26 July 2018 / Revised: 8 August 2018 / Accepted: 11 August 2018 / Published: 15 August 2018
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Abstract
Enzyme immobilization by multipoint covalent attachment on supports activated with aliphatic aldehyde groups (e.g., glyoxyl agarose) has proven to be an excellent immobilization technique for enzyme stabilization. Borohydride reduction of immobilized enzymes is necessary to convert enzyme–support linkages into stable secondary amino groups
[...] Read more.
Enzyme immobilization by multipoint covalent attachment on supports activated with aliphatic aldehyde groups (e.g., glyoxyl agarose) has proven to be an excellent immobilization technique for enzyme stabilization. Borohydride reduction of immobilized enzymes is necessary to convert enzyme–support linkages into stable secondary amino groups and to convert the remaining aldehyde groups on the support into hydroxy groups. However, the use of borohydride can adversely affect the structure–activity of some immobilized enzymes. For this reason, 2-picoline borane is proposed here as an alternative milder reducing agent, especially, for those enzymes sensitive to borohydride reduction. The immobilization-stabilization parameters of five enzymes from different sources and nature (from monomeric to multimeric enzymes) were compared with those obtained by conventional methodology. The most interesting results were obtained for bacterial (R)-mandelate dehydrogenase (ManDH). Immobilized ManDH reduced with borohydride almost completely lost its catalytic activity (1.5% of expressed activity). In contrast, using 2-picoline borane and blocking the remaining aldehyde groups on the support with glycine allowed for a conjugate with a significant activity of 19.5%. This improved biocatalyst was 357-fold more stable than the soluble enzyme at 50 °C and pH 7. The results show that this alternative methodology can lead to more stable and active biocatalysts. Full article
(This article belongs to the Special Issue Immobilization of Enzymes)
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