ORCID Profile
0000-0003-0078-5904
Current Organisations
Luleå University of Technology
,
National Technical University of Athens
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Publisher: MDPI AG
Date: 04-12-2019
DOI: 10.3390/CATAL9121023
Abstract: There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from in idual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society’s increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.
Publisher: MDPI AG
Date: 09-08-2023
Abstract: (1) Background: Bacterial nanocellulose (BNC) has gained in popularity over the years due to its outstanding properties such as renewability, biocompatibility, and bioavailability, and its use as an eco-friendly material of the future for replacing petrochemical products. (2) Methods: This research refers to the utilization of lignocellulose coming from wood waste via enzymatic hydrolysis to produce biopolymer BNC with an accumulation rate of 0.09 mg/mL/day. Besides its significant contribution to the sustainability, circularity, and valorization of biomass products, the obtained BNC was functionalized through the adsorption of black raspberry extract (BR) by simple soaking. (3) Results: BR contained 77.25 ± 0.23 mg GAE/g of total phenolics and 27.42 ± 0.32 mg CGE/g of total anthocyanins. The antioxidant and antimicrobial activity of BR was evaluated by DPPH (60.51 ± 0.18 µg/mL) and FRAP (1.66 ± 0.03 mmol Fe2+/g) and using a standard disc diffusion assay, respectively. The successful synthesis and interactions between BNC and BR were confirmed by FTIR analysis, while the morphology of the new nutrient-enriched material was investigated by SEM analysis. Moreover, the in vitro release kinetics of a main active compound (cyanidin-3-O-rutinoside) was tested in different release media. (4) Conclusions: The upcycling process of lignocellulose into enriched BNC has been demonstrated. All findings emphasize the potential of BNC–BR as a sustainable food industry material.
Publisher: MDPI AG
Date: 26-01-2023
Abstract: Polyurethanes (PUs) are an exceedingly heterogeneous group of plastic polymers, widely used in a variety of industries from construction to medical implants. In the past decades, we have witnessed the accumulation of PU waste and its detrimental environmental impacts. PUs have been identified as one of the most toxic polymers leaching hazardous compounds derived both from the polymer itself and the additives used in production. Further environmental impact assessment, identification and characterization of substances derived from PU materials and establishing efficient degradation strategies are crucial. Thus, a selection of eight synthetic model compounds which represent partial PU hydrolysis products were synthesized and characterized both in terms of toxicity and suitability to be used as substrates for the identification of novel biocatalysts for PU biodegradation. Overall, the compounds exhibited low in vitro cytotoxicity against a healthy human fibroblast cell line and virtually no toxic effect on the nematode Caenorhabditis elegans up to 500 µg mL−1, and two of the substrates showed moderate aquatic ecotoxicity with EC50 values 53 µg mL−1 and 45 µg mL−1, respectively, on Aliivibrio fischeri. The compounds were successfully applied to study the mechanism of ester and urethane bond cleaving preference of known plastic-degrading enzymes and were used to single out a novel PU-degrading biocatalyst, Amycolatopsis mediterranei ISP5501, among 220 microbial strains. A. mediterranei ISP5501 can also degrade commercially available polyether and polyester PU materials, reducing the average molecular number of the polymer up to 13.5%. This study uncovered a biocatalyst capable of degrading different types of PUs and identified potential enzymes responsible as a key step in developing biotechnological process for PU waste treatment options.
Publisher: MDPI AG
Date: 05-2020
Abstract: Biocatalysis has developed new molecular tools for the improvement of a wide range of bioprocesses that diminish raw material and energy consumption, while reducing or eliminating the formation of byproducts that might be hazardous to human health and the environment [...]
Publisher: MDPI
Date: 09-11-2020
Publisher: MDPI AG
Date: 12-06-2021
Abstract: We describe herein the synthesis and laccase mediated oxidation of six novel 1,4-dihydropyridine (DHP)-based hexahydroquinolines (DHP1-DHP3) and decahydroacridines (DHP4-DHP6). We employed different laccase enzymes with varying redox potential to convert DHP1-DHP3 and DHP4-DHP6 to the corresponding pyridine-containing tetrahydroquinoline and octahydroacridine derivatives, respectively. Intensively coloured products were detected in all biocatalytic reactions using laccase from Trametes versicolor (TvLacc), possibly due to the presence of conjugated chromophores formed in products after oxidation. The NMR assessment confirmed that the oxidation product of DHP1 was its corresponding pyridine-bearing tetrahydroquinoline derivative. Laccase from Bacillus subtillis (BacillusLacc) was the most efficient enzyme for this group of substrates using HPLC assessment. Overall, it could be concluded that DHP2 and DHP5, bearing catecholic structures, were easily oxidized by all tested laccases, while DHP3 and DHP6 containing electron-withdrawing nitro-groups are not readily oxidized by laccases. DHP4 with decahydroacridine moiety consisting of three condensed six-membered rings that contribute not only to the volume but also to the higher redox potential of the substrate rendered this compound not to be biotransformed with any of the mentioned enzymes. Overall, we showed that multiple analytical approaches are needed in order to assess biocatalytical reactions.
No related grants have been discovered for Evangelos Topakas.