Advances in Enzyme Immobilization

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

Deadline for manuscript submissions: closed (30 September 2021) | Viewed by 7201

Special Issue Editors


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Guest Editor
Department of Micro, Nano and Bioprocess Engineering, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland
Interests: applied biotechnology; bioprocess engineering; biocatalysis; enzyme purification; immobilization of enzymes and other bioactive compounds; functional materials; hydrogels

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Guest Editor
Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Bloco 709, CEP 60455760, Fortaleza 60000-000, CE, Brazil
Interests: biocatalysis; enzyme immobilization; bioprocess engineering and biochemical reaction engineering
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Special Issue Information

Dear Colleagues,

Enzyme immobilization is still on the top of the research list in the field of applied biotechnology. Currently, attention is focused on conducting manufacturing processes using clean and eco-friendly technologies, which can be ensured through the application of biocatalysis.

Through the use of variety of immobilization techniques and supports, efficient industrial biocatalysts can be produced. The application of immobilized enzymes has many tangible benefits like the reusability of these biocatalysts without significant decline in catalytic activity and their lower susceptibility to denaturation caused by various environmental factors (e.g., temperature, pH, and ionic strength). These enzyme preparations are successfully used in many branches including food processing, manufacturing of fine chemicals, medical diagnostics, pharmaceuticals production, cosmetics formulations, and agriculture and environmental protection.

Although this research field has been explored for many years, there are still many unsolved issues to be considered, novel strategies to be discovered, and unique approaches to be applied. Therefore, this Special Issue entitled 'Advances in Enzyme Immobilization' was created as an exchange platform for relevant developments in this scientific field. Research articles, review articles, as well as short communications are invited that describe the significance and potential of immobilized enzymes in a broad perspective of applied techniques, supports, and commercial uses.

Dr. Karolina Labus
Prof. Dr. Luciana R. B. Gonçalves
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.

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Keywords

  • Developments in enzyme immobilization strategies (e.g., multi-layer immobilization, co-immobilization, site-oriented immobilization);
  • Recent advances in supports used for enzyme immobilizations (e.g., biodegradable polymers, hydrogels, nanoparticles, metal–organic frameworks);
  • Properties of immobilized enzymes (e.g., highly improved stability, hyperactivation, targeted activity, other new functional properties);
  • Immobilized enzymes as effective industrial biocatalysts (e.g., heterogenous catalysis, processing conditions, bioreactors characterization, kinetics studies);
  • Recent development in applications of immobilized enzymes (e.g., enzymatic fuel cells, biosensors, bioactive coatings, novel industrial bioprocesses, innovative biomedical and pharmaceutical applications);
  • Advances in the computational research on enzyme immobilization (e.g., molecular dynamics, macroscale process modeling)

Published Papers (2 papers)

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Research

15 pages, 2238 KiB  
Article
Encapsulated NOLA™ Fit 5500 Lactase—An Economically Beneficial Way to Obtain Lactose-Free Milk at Low Temperature
by Katarzyna Czyzewska and Anna Trusek
Catalysts 2021, 11(5), 527; https://doi.org/10.3390/catal11050527 - 21 Apr 2021
Cited by 8 | Viewed by 2911
Abstract
The current requirements of industrial biocatalysis are related to economically beneficial and environmentally friendly processes. Such a strategy engages low-temperature reactions. The presented approach is essential, especially in food processes, where temperature affects the quality and nutritional value foodstuffs. The subject of the [...] Read more.
The current requirements of industrial biocatalysis are related to economically beneficial and environmentally friendly processes. Such a strategy engages low-temperature reactions. The presented approach is essential, especially in food processes, where temperature affects the quality and nutritional value foodstuffs. The subject of the study is the hydrolysis of lactose with the commercial lactase NOLA™ Fit 5500 (NOLA). The complete decomposition of lactose into two monosaccharides gives a sweeter product, recommended for lactose intolerant people and those controlling a product’s caloric content. The hydrolysis reaction was performed at 15 °C, which is related to milk transportation and storage temperature. The enzyme showed activity over the entire range of substrate concentrations (up to 55 g/L lactose). For reusability and easy isolation, the enzyme was encapsulated in a sodium alginate network. Its stability allows carrying out six cycles of the complete hydrolysis of lactose to monosaccharides, lasting from two to four hours. During the study, the kinetic description of native and encapsulated NOLA was conducted. As a result, the model of competitive galactose inhibition and glucose mixed influence (competitive inhibition and activation) was proposed. The capsule size does not influence the reaction rate; thus, the substrate diffusion into capsules can be omitted from the process description. The prepared 4 mm capsules are easy to separate between cycles, e.g., using sieves. Full article
(This article belongs to the Special Issue Advances in Enzyme Immobilization)
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12 pages, 2124 KiB  
Article
Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols
by Dominika Stradomska, Monika Heba, Aleksandra Czernek, Nikodem Kuźnik, Danuta Gillner, Katarzyna Maresz, Wojciech Pudło, Andrzej Jarzębski and Katarzyna Szymańska
Catalysts 2021, 11(4), 518; https://doi.org/10.3390/catal11040518 - 20 Apr 2021
Cited by 10 | Viewed by 3083
Abstract
Dynamic kinetic resolution (DKR) is one of the most attractive methods for enantioselective synthesis. In the reported studies, lipase B from Candida antarctica (CALB) immobilized on siliceous mesoporous cellular foams (MCF) functionalized with different hydrophobic groups, and two ruthenium complexes with substituted cyclopentadienyl [...] Read more.
Dynamic kinetic resolution (DKR) is one of the most attractive methods for enantioselective synthesis. In the reported studies, lipase B from Candida antarctica (CALB) immobilized on siliceous mesoporous cellular foams (MCF) functionalized with different hydrophobic groups, and two ruthenium complexes with substituted cyclopentadienyl ligands were investigated as catalysts for the chemoenzymatic DKR of (rac)-1-phenylethanol, using Novozym 435 as a benchmark biocatalyst. Studies on the (rac)-1-phenylethanol transesterification reaction showed that CALB supported on MCFs grafted with methyl groups is a promising biocatalyst and isopropenyl acetate is a preferable acylation agent. Both Ru-complexes activated by K3PO4 or t-BuOK, proved to be effective catalysts of the racemization reaction. The final DKR experiments using all catalysts combinations singled out, gave 96% conversion, and (R)-1-phenylethyl acetate enantiomeric excess of 98% in 8 h using K3PO4 activator. Full article
(This article belongs to the Special Issue Advances in Enzyme Immobilization)
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