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Marine Algal Secondary Metabolites Are a Potential Pharmaceutical Resource for Human Society Developments
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Somasundaram Ambiga, Raja Suja Pandian, Lazarus Vijune Lawrence, Arjun Pandian, Ramu Arun Kumar, Bakrudeen Ali Ahmed Abdul
Marine fungus like Caldariomyces fumago synthesizes chloroperoxidase is distinctive among peroxidases in that it has a cysteinic thiolate as a fifth axial ligand of the heme rather than an imidazole ligand. This enzyme is extremely versatile: it catalyzes not only peroxidase reactions, but also catalase and monooxygenase reactions, and it’s almost unusual, in that in the presence of H2O2 and halide ions, it can catalyze halogenation reactions. A few oxidoreductases are now available for use in the textile, food, and other fields, and many are being actively developed for future commercialization. Industrial-technical, specialty chemical synthesis, environmental, food, pharmaceutical, and personal healthcare are some of the industries where oxidoreductase is used. Oxidoreductase-based biocatalysts fit well with the creation of highly effective, economic, and ecologically friendly industries because they are specialized, energy-saving, and biodegradable.
Greener Synthesis of Natural Products
Published in Ahindra Nag, Greener Synthesis of Organic Compounds, Drugs and Natural Products, 2022
Renata Kołodziejska, Renata Studzińska, Hanna Pawluk, Alina Woźniak
The next group of enzymes willingly used in asymmetric synthesis is oxidoreductases. Oxidoreductases include, among others: oxidases, hydroperoxidases, peroxidases, catalases, oxygenases, hydroxylases, dehydrogenases, and reductases. Of the oxidoreductases, dehydrogenases are particularly explored, which oxidize primary and secondary alcohols and reduce the carbonyl double bond to form an alcohol moiety. Oxygenases to carry out the reaction need oxygen as a co-substrate, catalyze the oxidation reactions of C-H and C=C binding, belong to the second important subgroup of oxidoreductases used in asymmetric synthesis. They are divided into dioxygenases, which incorporate two oxygen atoms into the substrate, and monooxygenases catalyze the incorporation of one oxygen atom into the hydroxylated substrate. In contrast, oxidases, enzymes that catalyze the transfer of hydrogen to oxygen, resulting in the formation of water or hydrogen peroxide, and reductases, which reduce olefins to alkanes, are used to a small extent in biosynthesis.
Role of Enzymes in Bioremediation of Organic Pollutants
Published in M.H. Fulekar, Bhawana Pathak, Bioremediation Technology, 2020
Smita Chaudhry, Rashmi Paliwal
Oxidoreductases catalyze the transfer of electrons from one molecule, the donor (reductant), to another compound known as the electron acceptor (oxidant). This group of enzymes usually utilizes NADP or NAD+ as cofactors. The contaminants are thus oxidized to harmless compounds during the oxidation-reduction reactions (Karigar and Rao, 2011). Oxidoreductases are further classified into 22 subclasses of enzymes. The oxidoreductase enzymatic system includes peroxidases (EC 1.11; act on the peroxide as an acceptor), dioxygenases (EC 1.14; act on the paired donor with the incorporation of molecular oxygen), and laccases (EC 1.15; act on the superoxide radical as an acceptor). These subclasses of oxidoreductases play important role in transformation of the organic compounds (Ali et al., 2017). Oxygenases are the EC 1 group of enzymes classified under oxidoreductase, catalyze the oxidation of organic compounds by transferring oxygen from molecular oxygen (O2), and utilize FAD/NADH/NADPH as the cosubstrate (Karigar and Rao, 2011). Oxygenases thus cleave the aromatic ring and increase the reactivity and water solubility of organic compounds (Arora et al., 2009). These enzymes may transfer one or both the oxygen atoms of the O2 molecule to the substrate, on the basis of which these are classified as monooxygenases and dioxygenases.
A contemporary review of enzymatic applications in the remediation of emerging estrogenic compounds
Published in Critical Reviews in Environmental Science and Technology, 2022
Jakub Zdarta, Luong N. Nguyen, Katarzyna Jankowska, Teofil Jesionowski, Long D. Nghiem
Immobilized oxidoreductases may be used in a variety of reactor configurations, which in general can be divided into two types according to their operational mode: batch and continuous. Batch reactors are frequently used due to their simplicity, easy process control and flexibility (Srikanlayanukul et al., 2016). Batch reactor types have been used for the removal of estrogens from water solutions and wastewaters, enabling the efficient removal of these compounds over a wide range of process conditions, even in long-term processes with relatively high efficiencies. The inability to achieve total removal of pollutants results from several drawbacks of batch systems, which include limited contact time between the immobilized enzyme and the substrate, diffusional limitations, and enzyme inhibition (Boudrant et al., 2020; Oh & Lim, 2019). Furthermore, the separation of biocatalysts from the postreaction mixture may be complicated, and the reusability of oxidoreductases in batch reactors has been shown to be limited (Ai et al., 2017; Lacerda et al., 2019).
A comprehensive review on enzymatic degradation of the organophosphate pesticide malathion in the environment
Published in Journal of Environmental Science and Health, Part C, 2019
Smita S. Kumar, Pooja Ghosh, Sandeep K. Malyan, Jyoti Sharma, Vivek Kumar
Oxidoreductases are a broad group of enzymes that facilitate the catalysis of electron transfer from one molecule to another, i.e. from the electron donor (the reductant) to the electron acceptor (the oxidant). Oxidoreductases usually require the addition of extraneous compounds as cofactors that can act either as electron acceptors or donors or both.9 Oxidation gives rise to alkyl sulfonate whereas hydrolytic reaction leads to the formation of alkyl thiols. In some of the organophosphorus compounds, transformation occurs via oxidative desulfuration by mixed-function oxidases while in others it is carried out by carboxylesterases. Oxidoreductase was found to be involved in the conversion of malathion to phosphorodithioic acid and phosphorothioic acid.63,113
Transesterification of vegetable oils into biodiesel by an immobilized lipase: a review
Published in Biofuels, 2023
Akossi Moya Joëlle Carole, Kouassi Konan Edmond, Abolle Abollé, Kouassi Esaie Kouadio Appiah, Yao Kouassi Benjamin
Enzymes are thermolabile proteins, biocatalysts in metabolic reactions. They act at low concentration and have a specificity of action. In modern biotechnology, enzymes catalyze reactions of interest to different industries, such as food, energy, medical or chemical industries. They are classified into seven main categories: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases, and translocases [46–48]: Oxidoreductases catalyze electron and proton transfers from a donor to a receptor.Example: superoxide anion and hydrogen peroxide.Transferases catalyze the transfer of groups.Example: glutathione S-transferases.Hydrolases catalyze the hydrolysis reactions of molecules.Example: lipases, esterases, proteases, amidases.Lyases catalyze decomposition reactions in which a C-C, C-O, C-N or other bond is broken without hydrolysis or oxidation.Example: fructose, bisphosphate, aldolase.Isomerases catalyze the transfer of groups in the same molecule to produce isomeric forms.Example: triose-phosphate isomerase.Ligases catalyze the joining of two molecules by new covalent bonds with concomitant hydrolysis of Adenosine-triphosphate (ATP) or other similar molecules.Example: glutamine synthetase.Translocases catalyze the movement of ions or molecules across cell membranes in general. Example: extern mitochondrial membrane.