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Biocatalytic Reduction of Organic Compounds by Marine-Derived Fungi
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Gabriel S. Baia, David E. Q. Jimenez, André Luiz Meleiro Porto
The research progress in biocatalyst research shows increasing production rates with methodology optimization to improve the catalytic properties of fungi and enzymes in the chemical and pharmacological industries. Several fungi and enzymes have been applied effectively in organic synthesis to the production of high-value chemicals and pharmaceutical intermediates using biocatalytic methods to obtain compounds with enantioselectivity and can be seen as increasingly important tools in asymmetric organic synthesis.
Green-Synthesized Nanoparticles as Potential Sensors for Health Hazardous Compounds
Published in Richard L. K. Glover, Daniel Nyanganyura, Rofhiwa Bridget Mulaudzi, Maluta Steven Mufamadi, Green Synthesis in Nanomedicine and Human Health, 2021
Rachel Fanelwa Ajayi, Sphamandla Nqunqa, Yonela Mgwili, Siphokazi Tshoko, Nokwanda Ngema, Germana Lyimo, Tessia Rakgotho, Ndzumbululo Ndou, Razia Adam
Biotransformation is a widely used method in green chemistry, and it massively contributes to the development of chiral chemistry in aqueous medium merging the constraints enforced by the efficient synthesis with the constraints related in respect to the environment (Veitía and Ferroud, 2015). This method deals with the use of a biocatalyst for the mediation of a chemical reaction and for the synthesis of an organic chemical. Biotransformation is currently playing a crucial role in many industries, including animal feedstock, chiral drug formation and vitamin production. Even the use of microbes and enzyme for synthesis is expected to grow enormously since the industries are being forced by the public to shift toward ‘‘green chemistry’’, which uses safer and cleaner chemicals in their manufacturing processes and produces less toxic effluents (Doble et al., 2004).
Hydrolytic Enzymes for the Synthesis of Pharmaceuticals
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Sergio González-Granda, Vicente Gotor-Fernández
From the enzyme toolbox, lipases have attracted great attention due to their versatility in both aqueous and organic solvents. However, substrate specificity and the necessity for 100% conversion into a determined single enantiomer are scopes that hydrolases cannot always achieve. Fortunately, two efficient alternatives can be employed: (i) the modification of the biocatalyst by immobilisation techniques or rational design, opening up new possibilities to create more robust and versatile biocatalysts; (ii) considering other enzyme classes such as alcohol dehydrogenases and transaminases, which can provide complementary access for those reactions in which hydrolases present practical limitations (Albarrán-Velo et al., 2018).
An update on late-stage functionalization in today’s drug discovery
Published in Expert Opinion on Drug Discovery, 2023
Andrew P. Montgomery, Jack M. Joyce, Jonathan J. Danon, Michael Kassiou
The final challenge is to overcome the unique issues facing the lesser-developed reaction manifolds. Unlocking the full potential of these reaction modes will enable access to completely new reactivity and broaden the scope of their applications. Dual photochemical/metal-catalyzed C–H functionalization has been demonstrated as a formidable technique for invoking radical initiation, however, the application of metallophotocatalysis to generate other reactive intermediates known to be accessible under mild light irradiation (e.g. anions, cations, carbenes, etc.) remains underdeveloped [22]. Despite the significant achievements of electrochemical-mediated transition metal catalysis in pharmaceutical development, applications of robust and transferable C–H functionalization remain limited, inhibiting the incorporation of electrochemical LSF in drug discovery [23]. Biocatalysis has significant potential in medicinal chemistry and process chemistry as enzymatic optimization improves; however, previous examples of transformations possessing high reaction selectivity have also sustained a reduction in scope due to biocatalyst specialization [24]. Future developments in protein engineering and genome mining are poised to overcome this barrier and bring biocatalytic manifolds closer to true LSF applications, while current efforts in metallophotoredox and electrochemical catalysis are expanding the functionality and breadth of LSF transformations step-by-step.
The first and low cost copper Schiff base/manganese oxide bio nanocomposite from unwanted plants as a robust industrial catalyst
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2020
Atena Naeimi, Sedighe Abbasspour, Seyedeh Atekeh Torabizadeh
Recovery and the catalytic activity are imperative options for the industrial application of this biocatalyst. For this aim, the structure of catalyst must be unchanged. A comparison of the FT-IR spectra of the used Mn3O4/CuL bio nanocolloid (six recovery cycles) with those of the fresh catalyst showed that the structure of the catalyst remained almost completely intact (Figure 7(a)). On the other hand, the reusability of the Mn3O4/CuL bio nanocolloid was explored in the oxidation of benzyl alcohol. When the reactions were completed, the nanocolloid was separated by centrifugation after addition of the ethyl acetate. Recovered catalyst in dry state was used for the next runs. Stability as well as the activity of it was investigated and Mn3O4/CuL bionanocolloid was recycled for six times. Remarkable results (100–90%) of benzaldehyde were gained showing excellent catalytic activity of nanocolloid without noticeable loss (Figure 7(b)).
Alternative method to improve the ethyl valerate yield using an immobilised Burkholderia cepacia lipase
Published in Journal of Microencapsulation, 2019
Wellington Correa Moreira, Alfredo Luís Pereira Elias, Wislei Riuper Osório, Giovana Silva Padilha
The highest performance is that the concatenated enzyme loading (200mg/mL), the substrate concentration (500mM) and a period time higher than 72h are considered (titration method). However, the GC values indicate no substantial yielding values. The results shown in Figure 3 indicate that with a lower enzyme loading (100mg/mL) and the substrate concentration (100mM), a GC value in the same magnitude is reached. This seems to be associated with the low substrate concentration minimising the water generated during the reaction. In this case, the decrease in the water concentration favours the right reaction direction (ethyl valerate synthesis). Another observation is that the increasing of the substrate concentrations leads to an enzyme inactivation as a terminal inhibitor of the lipases (alcohol) or an acidification of the micro aqueous interface (acid) is prevalent. Consequently, a lower quantity of the reagents and biocatalyst to a more economical feasible processing is induced.