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Contribution of Enzyme Catalysis to the Achievement of the UN Sustainable Development Goals

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (31 December 2024) | Viewed by 18656

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Guest Editor
Institute of Process Engineering in Life Sciences, Karlsruhe Institute of Technology, Fritz-Haber-Weg 4, 76131 Karlsruhe, Germany
Interests: intensification of bioprocesses; enzyme catalysis; CO2 conversion; microbial and enzymatic electrosynthesis; nonconventional production of organisms; bioprocess engineering
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Special Issue Information

Dear Colleagues,

The Sustainable Development Goals (SDGs), set up by the United Nations General Assembly in 2015, are a collection of 17 interlinked goals designed to be a "shared blueprint for peace and prosperity for people and the planet, now and into the future". Therefore, global efforts should focus on achieving these goals. Enzyme catalysis could affect the achievement of different SDGs, in particular: SDG 2—zero hunger; SDG 3—good health and well-being; SDG 7—affordable and clean energy; SDG 9—industry innovation and infrastructure; SDG 12—responsible consumption and production; SDG 13—climate action; SDG 14—life below water; and SDG 15—life on land. The technological aspects could include, for instance, the reduction in resource use (substrates, energy, and water), the conversion of harmful or poorly degradable substances, the generation of sustainably produced energy, and the production of pharmaceuticals and their precursors. The aim of this Special Issue is to show exemplarily examples of how enzyme technologies could contribute to the achievement of the SDGs. All authors have to clearly demonstrate the relevance of their contributions to the SDGs.

Prof. Dr. Dirk Holtmann
Guest Editor

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Keywords

  • enzymes
  • enzyme catalysis
  • biotransformation
  • sustainability
  • Sustainable Development Goals (SDGs)

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Published Papers (7 papers)

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Editorial

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5 pages, 218 KiB  
Editorial
Contribution of Enzyme Catalysis to the Achievement of the United Nations’ Sustainable Development Goals
by Dirk Holtmann, Frank Hollmann and Britte Bouchaut
Molecules 2023, 28(10), 4125; https://doi.org/10.3390/molecules28104125 - 16 May 2023
Cited by 3 | Viewed by 1852
Abstract
In September 2015, the United Nations General Assembly established the 2030 Agenda for Sustainable Development, which includes 17 Sustainable Development Goals (SDGs) [...] Full article

Research

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15 pages, 4896 KiB  
Article
Rational Design of Enzymatic Electrodes: Impact of Carbon Nanomaterial Types on the Electrode Performance
by Miroslava Varničić, Tim-Patrick Fellinger, Maria-Magdalena Titirici, Kai Sundmacher and Tanja Vidaković-Koch
Molecules 2024, 29(10), 2324; https://doi.org/10.3390/molecules29102324 - 15 May 2024
Cited by 1 | Viewed by 1356
Abstract
This research focuses on the rational design of porous enzymatic electrodes, using horseradish peroxidase (HRP) as a model biocatalyst. Our goal was to identify the main obstacles to maximizing biocatalyst utilization within complex porous structures and to assess the impact of various carbon [...] Read more.
This research focuses on the rational design of porous enzymatic electrodes, using horseradish peroxidase (HRP) as a model biocatalyst. Our goal was to identify the main obstacles to maximizing biocatalyst utilization within complex porous structures and to assess the impact of various carbon nanomaterials on electrode performance. We evaluated as-synthesized carbon nanomaterials, such as Carbon Aerogel, Coral Carbon, and Carbon Hollow Spheres, against the commercially available Vulcan XC72 carbon nanomaterial. The 3D electrodes were constructed using gelatin as a binder, which was cross-linked with glutaraldehyde. The bioelectrodes were characterized electrochemically in the absence and presence of 3 mM of hydrogen peroxide. The capacitive behavior observed was in accordance with the BET surface area of the materials under study. The catalytic activity towards hydrogen peroxide reduction was partially linked to the capacitive behavior trend in the absence of hydrogen peroxide. Notably, the Coral Carbon electrode demonstrated large capacitive currents but low catalytic currents, an exception to the observed trend. Microscopic analysis of the electrodes indicated suboptimal gelatin distribution in the Coral Carbon electrode. This study also highlighted the challenges in transferring the preparation procedure from one carbon nanomaterial to another, emphasizing the importance of binder quantity, which appears to depend on particle size and quantity and warrants further studies. Under conditions of the present study, Vulcan XC72 with a catalytic current of ca. 300 µA cm−2 in the presence of 3 mM of hydrogen peroxide was found to be the most optimal biocatalyst support. Full article
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14 pages, 2132 KiB  
Article
Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization
by Danivia Endi S. Souza, Lucas M. F. Santos, João P. A. Freitas, Lays C. de Almeida, Jefferson C. B. Santos, Ranyere Lucena de Souza, Matheus M. Pereira, Álvaro S. Lima and Cleide M. F. Soares
Molecules 2024, 29(3), 628; https://doi.org/10.3390/molecules29030628 - 29 Jan 2024
Cited by 5 | Viewed by 1956
Abstract
This work presents a framework for evaluating hybrid nanoflowers using Burkholderia cepacia lipase. It was expanded on previous findings by testing lipase hybrid nanoflowers (hNF-lipase) formation over a wide range of pH values (5–9) and buffer concentrations (10–100 mM). The free enzyme activity [...] Read more.
This work presents a framework for evaluating hybrid nanoflowers using Burkholderia cepacia lipase. It was expanded on previous findings by testing lipase hybrid nanoflowers (hNF-lipase) formation over a wide range of pH values (5–9) and buffer concentrations (10–100 mM). The free enzyme activity was compared with that of hNF-lipase. The analysis, performed by molecular docking, described the effect of lipase interaction with copper ions. The morphological characterization of hNF-lipase was performed using scanning electron microscopy. Fourier Transform Infrared Spectroscopy performed the physical–chemical characterization. The results show that all hNF-lipase activity presented values higher than that of the free enzyme. Activity is higher at pH 7.4 and has the highest buffer concentration of 100 mM. Molecular docking analysis has been used to understand the effect of enzyme protonation on hNF-lipase formation and identify the main the main binding sites of the enzyme with copper ions. The hNF-lipase nanostructures show the shape of flowers in their micrographs from pH 6 to 8. The spectra of the nanoflowers present peaks typical of the amide regions I and II, current in lipase, and areas with P–O vibrations, confirming the presence of the phosphate group. Therefore, hNF-lipase is an efficient biocatalyst with increased catalytic activity, good nanostructure formation, and improved stability. Full article
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10 pages, 1361 KiB  
Article
Enzymatic Carboxylation of Resorcinol in Aqueous Triethanolamine at Elevated CO2 Pressure
by Daniel Ohde, Benjamin Thomas, Paul Bubenheim and Andreas Liese
Molecules 2024, 29(1), 25; https://doi.org/10.3390/molecules29010025 - 19 Dec 2023
Cited by 1 | Viewed by 1255
Abstract
The fixation of CO2 by enzymatic carboxylation for production of valuable carboxylic acids is one way to recycle carbon. Unfortunately, this type of reaction is limited by an unfavourable thermodynamic equilibrium. An excess of the C1 substrate is required to increase conversions. [...] Read more.
The fixation of CO2 by enzymatic carboxylation for production of valuable carboxylic acids is one way to recycle carbon. Unfortunately, this type of reaction is limited by an unfavourable thermodynamic equilibrium. An excess of the C1 substrate is required to increase conversions. Solvents with a high CO2 solubility, such as amines, can provide the C1 substrate in excess. Here, we report on the effect of CO2 pressures up to 1100 kPa on the enzymatic carboxylation of resorcinol in aqueous triethanolamine. Equilibrium yields correlate to the bicarbonate concentration. However, inhibition is observed at elevated pressure, severely reducing the enzyme activity. The reaction yields were reduced at higher pressures, whereas at ambient pressure, higher yields were achieved. Overall, CO2 pressures above 100 kPa have been demonstrated to be counterproductive for improving the biotransformation, as productivity decreases rapidly for only a modest improvement in conversion. It is expected that CO2 carbamylation intensifies at elevated CO2 pressures, causing the inhibition of the enzyme. To further increase the reaction yield, the in situ product precipitation is tested by the addition of the quaternary ammonium salt tetrabutylammonium bromide. Full article
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17 pages, 2244 KiB  
Article
Enzyme-Assisted Extraction of Ulvan from the Green Macroalgae Ulva fenestrata
by Ana Malvis Romero, José Julián Picado Morales, Leon Klose and Andreas Liese
Molecules 2023, 28(19), 6781; https://doi.org/10.3390/molecules28196781 - 23 Sep 2023
Cited by 7 | Viewed by 4704
Abstract
Ulvan is a sulfated polysaccharide extracted from green macroalgae with unique structural and compositional properties. Due to its biocompatibility, biodegradability, and film-forming properties, as well as high stability, ulvan has shown promising potential as an ingredient of biopolymer films such as sustainable and [...] Read more.
Ulvan is a sulfated polysaccharide extracted from green macroalgae with unique structural and compositional properties. Due to its biocompatibility, biodegradability, and film-forming properties, as well as high stability, ulvan has shown promising potential as an ingredient of biopolymer films such as sustainable and readily biodegradable biomaterials that could replace petroleum-based plastics in diverse applications such as packaging. This work investigates the potential of Ulva fenestrata as a source of ulvan. Enzyme-assisted extraction with commercial cellulases (Viscozyme L and Cellulysin) and proteases (Neutrase 0.8L and Flavourzyme) was used for cell wall disruption, and the effect of the extraction time (3, 6, 17, and 20 h) on the ulvan yield and its main characteristics (molecular weight, functional groups, purity, and antioxidant capacity) were investigated. Furthermore, a combined process based on enzymatic and ultrasound extraction was performed. Results showed that higher extraction times led to higher ulvan yields, reaching a maximum of 14.1% dw with Cellulysin after 20 h. The combination of enzymatic and ultrasound-assisted extraction resulted in the highest ulvan extraction (17.9% dw). The relatively high protein content in U. fenestrata (19.8% dw) makes the residual biomass, after ulvan extraction, a potential protein source in food and feed applications. Full article
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10 pages, 2460 KiB  
Article
Biocatalysis in Water or in Non-Conventional Media? Adding the CO2 Production for the Debate
by Pablo Domínguez de María, Selin Kara and Fabrice Gallou
Molecules 2023, 28(18), 6452; https://doi.org/10.3390/molecules28186452 - 6 Sep 2023
Cited by 17 | Viewed by 2535
Abstract
Biocatalysis can be applied in aqueous media and in different non-aqueous solutions (non-conventional media). Water is a safe solvent, yet many synthesis-wise interesting substrates cannot be dissolved in aqueous solutions, and thus low concentrations are often applied. Conversely, non-conventional media may enable higher [...] Read more.
Biocatalysis can be applied in aqueous media and in different non-aqueous solutions (non-conventional media). Water is a safe solvent, yet many synthesis-wise interesting substrates cannot be dissolved in aqueous solutions, and thus low concentrations are often applied. Conversely, non-conventional media may enable higher substrate loadings but at the cost of using (fossil-based) organic solvents. This paper determines the CO2 production—expressed as kg CO2·kg product−1—of generic biotransformations in water and non-conventional media, assessing both the upstream and the downstream. The key to reaching a diminished environmental footprint is the type of wastewater treatment to be implemented. If the used chemicals enable a conventional (mild) wastewater treatment, the production of CO2 is limited. If other (pre)treatments for the wastewater are needed to eliminate hazardous chemicals and solvents, higher environmental impacts can be expected (based on CO2 production). Water media for biocatalysis are more sustainable during the upstream unit—the biocatalytic step—than non-conventional systems. However, processes with aqueous media often need to incorporate extractive solvents during the downstream processing. Both strategies result in comparable CO2 production if extractive solvents are recycled at least 1–2 times. Under these conditions, a generic industrial biotransformation at 100 g L−1 loading would produce 15–25 kg CO2·kg product−1 regardless of the applied media. Full article
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Review

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18 pages, 1844 KiB  
Review
Enzyme Catalysis for Sustainable Value Creation Using Renewable Biobased Resources
by Roland Wohlgemuth
Molecules 2024, 29(23), 5772; https://doi.org/10.3390/molecules29235772 - 6 Dec 2024
Viewed by 3935
Abstract
Enzyme catalysis was traditionally used by various human cultures to create value long before its basic concepts were uncovered. This was achieved by transforming the raw materials available from natural resources into useful products. Tremendous scientific and technological progress has been made globally [...] Read more.
Enzyme catalysis was traditionally used by various human cultures to create value long before its basic concepts were uncovered. This was achieved by transforming the raw materials available from natural resources into useful products. Tremendous scientific and technological progress has been made globally in understanding what constitutes an enzyme; what reactions enzymes can catalyze; and how to search, develop, apply, and improve enzymes to make desired products. The useful properties of enzymes as nature’s preferred catalysts, such as their high selectivity, diversity, and adaptability, enable their optimal function, whether in single or multiple reactions. Excellent opportunities for the resource-efficient manufacturing of compounds are provided by the actions of enzymes working in reaction cascades and pathways within the same reaction space, like molecular robots along a production line. Enzyme catalysis plays an increasingly prominent role in industrial innovation and responsible production in various areas, such as green and sustainable chemistry and industrial or white biotechnology. Sources of inspiration include current manufacturing or supply chain challenges, the treasure of natural enzymes, and opportunities to engineer tailor-made enzymes. Making the best use of the power of enzyme catalysis is essential for changing how current products are manufactured; how renewable biobased resources can replace fossil-based resources; and improving the safety, health, and environmental aspects of manufacturing processes to support cleaner and more sustainable production. Full article
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