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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
Biocatalysis is linked to biotechnology which can be defined as an interdisciplinary area strongly linked to scientific and technological research, whose main objective is to develop processes and products using biological agents. For the application of biotechnological processes, knowledge is required in several areas, such as organic chemistry, physics, bioinformatics, mechanical engineering, catalysis, mathematics, materials science and biology (microbiology, molecular biology, biochemistry) [2].
Synthesis of Important Chiral Building Blocks for Pharmaceuticals Using Lactobacillus and Rhodococcus Alcohol Dehydrogenases
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Marion Rauter, Simon Krebs, Gotthard Kunze
Biocatalysts such as alcohol dehydrogenases can be used with mild reaction conditions (e.g., room temperature, atmospheric pressure, neutral pH) and are therefore a highly interesting alternative to traditional chemical synthesis. So-called biocatalysis is characterized by the utilization of renewable, biological degradable, non-toxic resources and includes the use of enzymes or whole microorganisms as biocatalysts. Enzymes work chemo-, regio-, and stereoselective. In the case of ADHs, they allow the formation of optical pure alcohols (Bornscheuer et al., 2012; de Carvalho, 2011; Muñoz Solano et al., 2012).
Pharmaceuticals: Some General Aspects
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Biocatalysis plays an important role in pharmaceutical and medical science concerning its various applications. Enzymes as well as whole cells are employed for the synthesis of chiral active pharmaceutical ingredients or key intermediates thereof as a sustainable alternative to traditional chemical methods. Several chapters of this volume address this topic. A number of enzymes, most of them nowadays produced by recombinant techniques and optimized with respect to their properties by directed evolution methods, are used for therapeutic purposes (Baldo, 2015). According to Yari et al. (2017), they may be subdivided into enzymes used in enzyme replacement therapy, in cancer treatment (e.g., for amino acid depletion therapy in cancer (Cantor et al., 2012)), enzymes for fibrinolysis, and those used topically for various treatments. A categorization proposed by Vellard (2003) is shown opposite. Several of these applications are discussed in Vol. 6 of this Series on Biocatalysis. The importance of therapeutic enzymes is underlined by the fact that the International Pharmaceutical Federation (FIP) founded an International Commission on Pharmaceutical Enzymes already in 1960. The safety of treatments based on therapeutic enzymes used for enzyme replacement therapy in lysosomal storage disorders has been discussed by Broomfield et al. (2016) with respect to immunological mechanisms involved in the development of anti-drug antibodies (see also the FDA Investigational Enzyme Replacement Therapy Products: Nonclinical Assessment Guidance for Industryhttp://www.fda.gov/Drugs/GuidanceComplianceRegulatoryInformation/Guidances/default.htm, 2015).
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.
Advances in biocatalytic and chemoenzymatic synthesis of nucleoside analogues
Published in Expert Opinion on Drug Discovery, 2022
Sebastian C. Cosgrove, Gavin J. Miller
Biocatalysis has, however, advanced to a point where enzymes can now be designed to be the perfect catalyst for a particular process [5]. The advent of directed evolution in the early 1990s revolutionized how chemists approached enzymatic transformations, with pioneers such as Arnold demonstrating how artificial evolutionary pressure could transform the function of a protein in extremely short timeframes [6]. Technological advances since then, in particular the power of computation to help understand protein dynamics and the significant reduction in the cost of DNA technologies (e.g., synthesis and sequencing), have delivered a myriad of methods for the efficient evolution of enzymes for synthetic chemistry. A landmark study involved engineering of a transaminase to synthesize the blockbuster diabetes treatment sitagliptin [7]. This enzyme underwent multiple rounds of evolution to deliver a mutant that could operate under conditions akin to that of a synthetic catalyst (200 g L−1 substrate loading, 50% DMSO v/v, 1 M amine donor) and deliver the final amine with perfect stereocontrol. What this study demonstrated was how enzymes could be pushed to function well beyond their natural limits, but still under ambient conditions with perfect selectivity obtained from natural evolution.
Bioconjugation as a smart immobilization approach for α-amylase enzyme using stimuli-responsive Eudragit-L100 polymer: a robust biocatalyst for applications in pharmaceutical industry
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Heidi Mohamed Abdel-Mageed, Rasha Ali Radwan, Nermeen Zakaria AbuelEzz, Hebatallah Ahmed Nasser, Aliaa Ali El Shamy, Rana M. Abdelnaby, Nesrine Abdelrehim EL Gohary
Enzymes are biodegradable biocatalysts that catalyze selective reactions under mild operating conditions. They are cost efficient with the ability to reduce environmental impact unlike conventional chemical processes and they do not produce undesirable waste [4]. However, the industrial applications of enzymes are immensely hindered by high production cost and the inherently sensitive nature of enzymes that compromise their storage shelf life and stability under operational conditions. In addition, enzymes are typically wasted after completion of the catalytic process. Though, regarding their catalytic nature, they still retain their enzymatic activity at the end of the reaction [4,5]. Immobilization is an age-old method of biocatalyst stabilization. Immobilization is a physical or a chemical process in which enzymes are fixed to or confined to a support, creating a heterogeneous immobilized enzyme system that mimics the enzyme natural mode in living cells. Immobilization allows the recovery of enzymes for re-use as biocatalyst which is highly advantageous for industrial applications [4,5]. The choice of the appropriate immobilization support and the efficient immobilization method is fundamental for effective industrial applications of immobilized enzymes [5,6]. In instances where the enzyme has to act on macromolecular substrates (heterogeneous media) it is highly important that the support does not represent a constraint to enzymatic reaction [7].