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Catalysts
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Enzyme Bioreactor Design
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Enzyme Bioreactor Design

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

Deadline for manuscript submissions: closed (20 September 2022) | Viewed by 22179

Special Issue Editors

Dr. Maria Elena Russo

E-Mail Website
Guest Editor
Istituto di Scienze e Tecnologie per l'Energia e la Mobilità Sostenibili-Consiglio Nazionale delle Ricerche, Napoli, Italy
Interests: biocatalysis; bioreactors; immobilized enzyme; biocatalyst kinetics
Special Issues, Collections and Topics in MDPI journals
Dr. Giuseppe Olivieri

E-Mail Website
Guest Editor
Bioprocess Engineering Group, Wageningen University and Research, 6700AA Wageningen, The Netherlands
Interests: biorefinery; bioreactor design; microalgae; bioprocess engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzyme catalysis has been exploited in many industrial applications from food to pharmaceutical sectors and can be extended even further to meet current societal and industrial needs. In particular, technologies for the immobilization of enzymes and their use as industrial biocatalysts in multiphase reactors offer many opportunities to develop new enzymatic processes in most fields with a central role in the establishment of green economy. Among these fields, biorefinery platforms, CO2 capture and utilization processes, bio-based productions of commodity chemicals can be enriched with novel strategies and technologies based on the use of enzyme biocatalysts. The successful development of enzymatic processes up to industrial scale is strongly related to the design of bioreactor configurations enabling the efficient use of the enzyme biocatalyst. This Special Issue will publish research and review articles addressing experimental and theoretical studies on enzyme bioreactors design and development. Contributions dealing with but not limited to enzyme bioreactors for the following applications are welcome:

- Biorefinery processes
- Novel enzyme technologies for CO2 utilization purposes
- Bio-based product, continuous production, and downstream integration
- Multiphase systems for enzyme use in non-aqueous solvents

Dr. Maria Elena Russo
Dr. Giuseppe Olivieri
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 2700 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

  • Bioreactors
  • Immobilized enzymes
  • Heterogeneous biocatalysis
  • Kinetics
  • Bio-based products

Published Papers (6 papers)

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Research

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32 pages, 4879 KiB  
Article
Durable and Versatile Immobilized Carbonic Anhydrase on Textile Structured Packing for CO2 Capture
by Jialong Shen, Yue Yuan and Sonja Salmon
Catalysts 2022, 12(10), 1108; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12101108 - 25 Sep 2022
Cited by 7 | Viewed by 2845
Abstract
High-performance carbon dioxide (CO2)-capture technologies with low environmental impact are necessary to combat the current climate change crisis. Durable and versatile “drop-in-ready” textile structured packings with covalently immobilized carbonic anhydrase (CA) were created as efficient, easy to handle catalysts for CO [...] Read more.
High-performance carbon dioxide (CO2)-capture technologies with low environmental impact are necessary to combat the current climate change crisis. Durable and versatile “drop-in-ready” textile structured packings with covalently immobilized carbonic anhydrase (CA) were created as efficient, easy to handle catalysts for CO2 absorption in benign solvents. The hydrophilic textile structure itself contributed high surface area and superior liquid transport properties to promote gas-liquid reactions that were further enhanced by the presence of CA, leading to excellent CO2 absorption efficiencies in lab-scale tests. Mechanistic investigations revealed that CO2 capture efficiency depended primarily on immobilized enzymes at or near the surface, whereas polymer entrapped enzymes were more protected from external stressors than those exposed at the surface, providing strategies to optimize performance and durability. Textile packing with covalently attached enzyme aggregates retained 100% of the initial 66.7% CO2 capture efficiency over 71-day longevity testing and retained 85% of the initial capture efficiency after 1-year of ambient dry storage. Subsequent stable performance in a 500 h continuous liquid flow scrubber test emphasized the material robustness. Biocatalytic textile packings performed well with different desirable solvents and across wide CO2 concentration ranges that are critical for CO2 capture from coal and natural gas-fired power plants, from natural gas and biogas for fuel upgrading, and directly from air. Full article
(This article belongs to the Special Issue Enzyme Bioreactor Design)
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17 pages, 2900 KiB  
Article
Potential and Scale-Up of Pore-Through-Flow Membrane Reactors for the Production of Prebiotic Galacto-Oligosaccharides with Immobilized β-Galactosidase
by Ines Pottratz, Ines Müller and Christof Hamel
Catalysts 2022, 12(1), 7; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12010007 - 22 Dec 2021
Cited by 8 | Viewed by 2318
Abstract
The production of prebiotics like galacto-oligosaccharides (GOS) on industrial scale is becoming more important due to increased demand. GOS are synthesized in batch reactors from bovine lactose using the cost intensive enzyme β-galactosidase (β-gal). Thus, the development of sustainable and more efficient production [...] Read more.
The production of prebiotics like galacto-oligosaccharides (GOS) on industrial scale is becoming more important due to increased demand. GOS are synthesized in batch reactors from bovine lactose using the cost intensive enzyme β-galactosidase (β-gal). Thus, the development of sustainable and more efficient production strategies, like enzyme immobilization in membrane reactors are a promising option. Activated methacrylatic monoliths were characterized as support for covalent immobilized β-gal to produce GOS. The macroporous monoliths act as immobilized pore-through-flow membrane reactors (PTFR) and reduce the influence of mass-transfer limitations by a dominating convective pore flow. Monolithic designs in the form of disks (0.34 mL) and for scale-up cylindric columns (1, 8 and 80 mL) in three different reactor operation configurations (semi-continuous, continuous and continuous with recirculation) were studied experimentally and compared to the free enzyme system. Kinetic data, immobilization efficiency, space-time-yield and long-term stability were determined for the immobilized enzyme. Furthermore, simulation studies were conducted to identify optimal operation conditions for further scale-up. Thus, the GOS yield could be increased by up to 60% in the immobilized PTFRs in semi-continuous operation compared to the free enzyme system. The enzyme activity and long-time stability was studied for more than nine months of intensive use. Full article
(This article belongs to the Special Issue Enzyme Bioreactor Design)
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15 pages, 2293 KiB  
Article
An Experimental Study on the Biological Fixation and Effective Use of Carbon Using Biogas and Bacterial Community Dominated by Methanotrophs, Methanol-Oxidizing Bacteria, and Ammonia-Oxidizing Bacteria
by I-Tae Kim, Kwang-Ho Ahn, Ye-Eun Lee, Yoonah Jeong, Jae-Roh Park, Dong-Chul Shin and Jinhong Jung
Catalysts 2021, 11(11), 1342; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11111342 - 08 Nov 2021
Cited by 5 | Viewed by 2557
Abstract
This study used biogas from a wastewater treatment plant and bacterial community where methanotrophs, Methylophilus, and ammonia-oxidizing bacteria clusters coexisted to propose an effective method for biological carbon fixation and nitrogen removal in wastewater treatment for carbon capture, utilization, and storage (CCUS). [...] Read more.
This study used biogas from a wastewater treatment plant and bacterial community where methanotrophs, Methylophilus, and ammonia-oxidizing bacteria clusters coexisted to propose an effective method for biological carbon fixation and nitrogen removal in wastewater treatment for carbon capture, utilization, and storage (CCUS). Biogas from wastewater treatment plant was provided, instead of purified CH4, to provide operation and maintenance conditions of bio-catalyst reaction for efficient biological carbon fixation by bacterial community using methane and CO2. This study assessed the conditions to induce type X methanotrophs that can use CO2 as a carbon source, as dominant species in the bacterial community and continuously and effectively supply reducing equivalents required for the conversion of CO2 to methanol within the system. Herein, the results of inducing efficient co-existence of methanotrophs, Methylophilus, and ammonia-oxidizing bacteria cluster in the bacterial community were shown. Full article
(This article belongs to the Special Issue Enzyme Bioreactor Design)
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11 pages, 2030 KiB  
Article
A Simple and Straightforward Method for Activity Measurement of Carbonic Anhydrases
by Werner Fuchs, Franziska Steger, Johanna Reich, Doris Ribitsch, Simon K.-M. R. Rittmann and Günther Bochmann
Catalysts 2021, 11(7), 819; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11070819 - 06 Jul 2021
Cited by 6 | Viewed by 5246
Abstract
Carbonic anhydrase (CA) is an enzyme of high interest due to its high implications relative to the medical and environmental sectors. In the current paper, an enzyme assay for the determination of CA activity is proposed and it is characterized by its simplicity [...] Read more.
Carbonic anhydrase (CA) is an enzyme of high interest due to its high implications relative to the medical and environmental sectors. In the current paper, an enzyme assay for the determination of CA activity is proposed and it is characterized by its simplicity and high practicability. It permits the straightforward comparison of CAs performance in physiological conditions. The methodology and the theoretical background of the evaluation method are explained in detail. Moreover, the presumed advantages over alternative assays are discussed. The assay has proven to be particularly useful for the screening of CA activity with respect to their application in CO2, capturing processes for further utilization or storage. Full article
(This article belongs to the Special Issue Enzyme Bioreactor Design)
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18 pages, 20608 KiB  
Article
Analytical Determination of the Optimal Feed Temperature for Hydrogen Peroxide Decomposition Process Occurring in Bioreactor with a Fixed-Bed of Commercial Catalase
by Ireneusz Grubecki
Catalysts 2021, 11(1), 35; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11010035 - 30 Dec 2020
Cited by 2 | Viewed by 2078
Abstract
The hydrogen peroxide-immobilized commercial catalase system was chosen to estimate the optimal feed temperature (OFT) for fixed-bed reactor (FXBR). This feed temperature was obtained based on analytical solution by maximizing the time-averaged substrate conversion under a constant feed flow rate and temperature constraints. [...] Read more.
The hydrogen peroxide-immobilized commercial catalase system was chosen to estimate the optimal feed temperature (OFT) for fixed-bed reactor (FXBR). This feed temperature was obtained based on analytical solution by maximizing the time-averaged substrate conversion under a constant feed flow rate and temperature constraints. In calculations a set of partial differential equations describing the conservation equation for fixed-bed reactor, assuming plug flow and kinetic equation for the rate of enzyme parallel deactivation was taken into account. The model is based on kinetic, and mass-transfer parameters estimated previously in a real decomposition process of hydrogen peroxide (HP). The simulation showed that the OFT is strongly dependent on hydrogen peroxide feed concentration, feed flow rate and diffusional resistances expressed by biocatalyst global effectiveness factor. It has been shown that the more significant diffusional resistances and the higher HP conversions are, the higher the optimal feed temperature is. The calculated values of the OFT were verified with the experimental results obtained in the model reactor at selected values of the feed flow rate. Presented analysis poses a significant simplification in a numerical computational procedure and can be very useful for engineers to select the temperature condition at which bioreactor productivity is expected to be maximal. Full article
(This article belongs to the Special Issue Enzyme Bioreactor Design)
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Review

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19 pages, 1742 KiB  
Review
Bioreactor and Bioprocess Design Issues in Enzymatic Hydrolysis of Lignocellulosic Biomass
by Giuseppe Olivieri, René H. Wijffels, Antonio Marzocchella and Maria Elena Russo
Catalysts 2021, 11(6), 680; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11060680 - 27 May 2021
Cited by 24 | Viewed by 5895
Abstract
Saccharification of lignocellulosic biomass is a fundamental step in the biorefinery of second generation feedstock. The physicochemical and enzymatic processes for the depolymerization of biomass into simple sugars has been achieved through numerous studies in several disciplines. The present review discusses the development [...] Read more.
Saccharification of lignocellulosic biomass is a fundamental step in the biorefinery of second generation feedstock. The physicochemical and enzymatic processes for the depolymerization of biomass into simple sugars has been achieved through numerous studies in several disciplines. The present review discusses the development of technologies for enzymatic saccharification in industrial processes. The kinetics of cellulolytic enzymes involved in polysaccharide hydrolysis has been discussed as the starting point for the design of the most promising bioreactor configurations. The main process configurations—proposed so far—for biomass saccharification have been analyzed. Attention was paid to bioreactor configurations, operating modes and possible integrations of this operation within the biorefinery. The focus is on minimizing the effects of product inhibition on enzymes, maximizing yields and concentration of sugars in the hydrolysate, and reducing the impact of enzyme cost on the whole process. The last part of the review is focused on an emerging process based on the catalytic action of laccase applied to lignin depolymerization as an alternative to the consolidated physicochemical pretreatments. The laccases-based oxidative process has been discussed in terms of characteristics that can affect the development of a bioreactor unit where laccases or a laccase-mediator system can be used for biomass delignification. Full article
(This article belongs to the Special Issue Enzyme Bioreactor Design)
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