Special Issue "Immobilization of Enzymes"

A special issue of Catalysts (ISSN 2073-4344).

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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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1300 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

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 (1 paper)

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Research

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
PDF Full-text (1323 KB) | HTML Full-text | XML Full-text | Supplementary Files
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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