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Catalysts
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Overcoming the Challenges in Biocatalytic Applications
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Overcoming the Challenges in Biocatalytic Applications

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

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 14541

Special Issue Editors

Dr. Martina Letizia Contente

E-Mail Website
Guest Editor
Department of Food, Environmental and Nutritiona Sciences (DeFENS), University of Milan, via mangiagalli 25, 20133 Milan, Italy
Interests: enzyme discovery; heterogeneous catalysis; enzyme immobilization; process intensification; process automation
Special Issues, Collections and Topics in MDPI journals
Dr. Ana I. Benítez-Mateos

E-Mail Website1 Website2
Guest Editor
Department of Chemistry and Biochemistry, University of Bern, 3012 Bern, Switzerland
Interests: sustainable biocatalysis; enzyme immobilization; single-particle analysis; enzyme stabilization; protein engineering

Special Issue Information

Dear Colleagues,

Enzymes are amazing catalysts in terms of selectivity (chemo-, regio-, and enantio-selectivity), sustainability, and biocompatibility. Although biocatalysis is considered a “hot topic” because of its potential, enzymatic reactions represent only a small fraction of the total industrial processing. The major drawbacks are related to poor enzyme stability when harsh reaction conditions are required (solvents, high temperature, acid or basic pH) as well as cost efficiency (mainly their production and reusability). There is a pressing demand to develop innovative strategies in order to reach the imposed standard for industrial applications and make biocatalysts a strategic addition to other catalysts in the chemist’s toolkit.

This Special Issue aims to overcome the perception that biocatalysis is inefficient compared with traditional chemical methods. Submissions are welcome in the following topics:

  • Novel materials and methodologies for enzyme/whole-cell immobilization;
  • Biocatalyst integration in continuous processes;
  • Hierarchical spatial organization of enzymes and cofactors;
  • Advances in the characterization and monitoring of biocatalyst performance;
  • Biocatalyst functionalization for enhanced stability;
  • Bioreactor engineering and downstream processing;
  • Biocatalyst reusability;
  • Catalysis innovation: biocatalyst evolution, enzyme discovery, computational design.

The contributions of emerging scientists (young leaders, first author PhD students) are highly promoted.

Dr. Martina Letizia Contente
Dr. Ana I. Benítez-Mateos
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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 2200 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 and whole-cell immobilization
  • Flow biocatalysis
  • Sustainable chemistry
  • Biocatalyst application
  • Operational stability
  • Process cost-efficiency

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Published Papers (4 papers)

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Research

19 pages, 2335 KiB  
Article
Immobilization-Stabilization of β-Glucosidase for Implementation of Intensified Hydrolysis of Cellobiose in Continuous Flow Reactors
by Celia Alvarez-Gonzalez, Victoria E. Santos, Miguel Ladero and Juan M. Bolivar
Catalysts 2022, 12(1), 80; https://doi.org/10.3390/catal12010080 - 11 Jan 2022
Cited by 11 | Viewed by 2582
Abstract
Cellulose saccharification to glucose is an operation of paramount importance in the bioenergy sector and the chemical and food industries, while glucose is a critical platform chemical in the integrated biorefinery. Among the cellulose degrading enzymes, β-glucosidases are responsible for cellobiose hydrolysis, the [...] Read more.
Cellulose saccharification to glucose is an operation of paramount importance in the bioenergy sector and the chemical and food industries, while glucose is a critical platform chemical in the integrated biorefinery. Among the cellulose degrading enzymes, β-glucosidases are responsible for cellobiose hydrolysis, the final step in cellulose saccharification, which is usually the critical bottleneck for the whole cellulose saccharification process. The design of very active and stable β-glucosidase-based biocatalysts is a key strategy to implement an efficient saccharification process. Enzyme immobilization and reaction engineering are two fundamental tools for its understanding and implementation. Here, we have designed an immobilized-stabilized solid-supported β-glucosidase based on the glyoxyl immobilization chemistry applied in porous solid particles. The biocatalyst was stable at operational temperature and highly active, which allowed us to implement 25 °C as working temperature with a catalyst productivity of 109 mmol/min/gsupport. Cellobiose degradation was implemented in discontinuous stirred tank reactors, following which a simplified kinetic model was applied to assess the process limitations due to substrate and product inhibition. Finally, the reactive process was driven in a continuous flow fixed-bed reactor, achieving reaction intensification under mild operation conditions, reaching full cellobiose conversion of 34 g/L in a reaction time span of 20 min. Full article
(This article belongs to the Special Issue Overcoming the Challenges in Biocatalytic Applications)
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10 pages, 1457 KiB  
Article
Agarose vs. Methacrylate as Material Supports for Enzyme Immobilization and Continuous Processing
by Ana I. Benítez-Mateos and Martina L. Contente
Catalysts 2021, 11(7), 814; https://doi.org/10.3390/catal11070814 - 2 Jul 2021
Cited by 23 | Viewed by 3399
Abstract
Enzyme immobilization has become a key strategy to improve the stability and recycling of biocatalysts, resulting in greener and more cost-efficient processes. The design of the immobilized catalysts is often focused only on the immobilization strategy, the binding chemistry between the enzyme and [...] Read more.
Enzyme immobilization has become a key strategy to improve the stability and recycling of biocatalysts, resulting in greener and more cost-efficient processes. The design of the immobilized catalysts is often focused only on the immobilization strategy, the binding chemistry between the enzyme and the support, while less attention has been paid to the physico-chemical properties of material supports. Selecting the best carrier for a specific application may greatly influence the performance of the biocatalytic reaction. Herein, we present a comparative study between the two most used material supports for protein immobilization, agarose and methacrylate. Hydrophilic agarose microbeads ensure higher retained enzymatic activity and better catalyst performance when hydrophobic compounds are involved in the biotransformation. Due to the high stickiness, lipophilic molecules represent a major limitation for methacrylate carriers. O2-dependent reactions, in contrast, must be carried out by immobilized enzymes on methacrylate supports due to the low mechanical stability of agarose under dehydration conditions. All these parameters were tested with a special focus on continuous-flow applications. Full article
(This article belongs to the Special Issue Overcoming the Challenges in Biocatalytic Applications)
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13 pages, 1478 KiB  
Article
Efficient Amino Donor Recycling in Amination Reactions: Development of a New Alanine Dehydrogenase in Continuous Flow and Dialysis Membrane Reactors
by David Roura Padrosa, Zoya Nisar and Francesca Paradisi
Catalysts 2021, 11(4), 520; https://doi.org/10.3390/catal11040520 - 20 Apr 2021
Cited by 14 | Viewed by 3809
Abstract
Transaminases have arisen as one of the main biocatalysts for amine production but despite their many advantages, their stability is still a concern for widespread application. One of the reasons for their instability is the need to use an excess of the amino [...] Read more.
Transaminases have arisen as one of the main biocatalysts for amine production but despite their many advantages, their stability is still a concern for widespread application. One of the reasons for their instability is the need to use an excess of the amino donor when trying to synthesise amines with unfavourable equilibria. To circumvent this, recycling systems for the amino donor, such as amino acid dehydrogenases or aldolases, have proved useful to push the equilibria while avoiding high amino donor concentrations. In this work, we report the use of a new alanine dehydrogenase from the halotolerant bacteria Halomonas elongata which exhibits excellent stability to different cosolvents, combined with the well characterised CbFDH as a recycling system of L-alanine for the amination of three model substrates with unfavourable equilibria. In a step forward, the amino donor recycling system has been co-immobilised and used in flow with success as well as re-used as a dialysis enclosed system for the amination of an aromatic aldehyde. Full article
(This article belongs to the Special Issue Overcoming the Challenges in Biocatalytic Applications)
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18 pages, 5159 KiB  
Article
Covalent Immobilization of Proteases on Polylactic Acid for Proteins Hydrolysis and Waste Biomass Protein Content Valorization
by Eleonora Calzoni, Alessio Cesaretti, Silvia Tacchi, Silvia Caponi, Roberto Maria Pellegrino, Francesca Luzi, Francesco Cottone, Daniele Fioretto, Carla Emiliani and Alessandro Di Michele
Catalysts 2021, 11(2), 167; https://doi.org/10.3390/catal11020167 - 26 Jan 2021
Cited by 15 | Viewed by 3444
Abstract
The recovery of the protein component and its transformation into protein hydrolysates, generally carried out chemically, gives great added value to waste biomasses. The production of protein hydrolysates through enzymatic catalysis would guarantee to lower the environmental impact of the process and raise [...] Read more.
The recovery of the protein component and its transformation into protein hydrolysates, generally carried out chemically, gives great added value to waste biomasses. The production of protein hydrolysates through enzymatic catalysis would guarantee to lower the environmental impact of the process and raise product quality, due to the reproducible formation of low molecular weight peptides, with interesting and often unexplored biological activities. The immobilization of the enzymes represents a good choice in terms of stability, recyclability and reduction of costs. In this context, we covalently linked proteases from Aspergillus oryzae to polylactic acid an eco-friendly biopolymer. The hydrolytic efficiency of immobilized enzymes was assessed testing their stability to temperature and over time, and checking the hydrolysis of model biomasses (casein and bovine serum albumin). Soybean waste extracts were also used as proof of principle. Full article
(This article belongs to the Special Issue Overcoming the Challenges in Biocatalytic Applications)
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