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Nanobiotechnology Advances in Bioreactors for Biodiesel Production
Published in Madan L. Verma, Nanobiotechnology for Sustainable Bioenergy and Biofuel Production, 2020
Bhaskar Birru, P. Shalini, Madan L. Verma
The lower greenhouse gas emission is achievable with the use of biodiesel as a renewable energy resource and it is derived from fatty acids and oil. To increase the yield of biodiesel, fatty acid, lipid synthesis and metabolic engineering approach are inevitable. The initial step in the fat synthesis is the conversion of actyl-CoA into Malonyl-CoA, catalyzed by acetyl-CoA carboxylase. The soxidation of NADPH requires fat synthesis, which occurs in the cytosol. The pyruvate dehydrogenase (PDH) and fatty acid oxidation pathways generate acetyl-CoA in mitochondria; it cannot be transported into the cytosol. Kerb’s cycle produces citrate in mitochondria, which is transported into the cytoplasm. Citrate breaks down into acetyl-CoA and oxalo acetate (OAA); this is catalyzed by ATP citrate lyase. The OAA converts into malate by malate dehydrogenase enzyme and NAD+. Subsequently, pyruvate is synthesized from malate and then it enters into mitochondria. This pyruvate is also produced through the glycolytic pathway. Transesterification of triacyl glycerol (TAG) produces biodiesel. TAG serves as energy storage in all cells and easily catabolized to provide metabolic energy. TAG contains three fatty acids and the glycerol molecule (Vuppaladadiyam et al. 2018).
Outdoor Air Pollution
Published in William J. Rea, Kalpana D. Patel, Reversibility of Chronic Disease and Hypersensitivity, Volume 4, 2017
William J. Rea, Kalpana D. Patel
Mitochondria have a proteome of approximately 1500 proteins.221 Nearly 1000 of these proteins have catalytic functions in cell metabolism such as citrate synthase or malate dehydrogenase. Under normal physiologic conditions, the concentrations of thousands of nutrients and metabolic substrates in mitochondria are closely governed by the collective kinetic constants (Km, Kcat, V, Hill coefficient, etc.) of all the enzymes responsible for transforming those metabolites. This has recently been computationally modeled in the Recon 1 and BiGG reconstructions of cell and organ metabolism.222,223 Only the primary structure of an enzyme is genetically determined. The activity of an enzyme at any instant in time is determined by ambient metabolic conditions. The environmental triggering agents, for example, the Km of citrate synthase for oxaloacetate is approximately 2 μM, but the enzyme is allosterically inhibited by ATP, NADH, acetyl-CoA, palmitoyl-CoA, and the product citric acid so the rate of converting oxaloacetate to citrate is changing minute to minute according to the condition of the cell.224 When the concentrations of substrates are perturbed by viral or microbial infection, disease, toxin, or nutritional excess, mitochondria sense this as a metabolic mismatch between the optimum concentration of those metabolites for a given tissue and the actual concentration. Thus the chemically sensitive patient due to its varied metabolism responds differently at different times. At times, they have more resistance and other times are very vulnerable. This function at times makes treatment doses of antigens and nutrients difficult to deliver due to the need for varying doses. Of course, medications, nutrients, and interdermal neutralization at varying times are fixed doses and may not function at times of crises unless they are primed over weeks and months when the organism is stable.
A dye-affinity cryogel membrane for malate dehydrogenase purification from Saccharomyces cerevisiae
Published in Journal of Biomaterials Science, Polymer Edition, 2020
Kamar Hamade, Ilgım Göktürk, Nilay Bereli, Deniz Türkmen, Assem Elkak, Adil Denizli
Malate dehydrogenase (MDH) is an isoenzyme found in many organisms, including yeast, bacteria, plants and animals, and is one of the most important enzymes in the metabolic pathways leading to a reversible oxidation of malate into oxaloacetate in both eukaryotic and prokaryotic organisms [1, 2]. MDH has several advantages such as being commonly used a reagent for the determination of malic acid concentration in tissue and food samples, aspartate transferase in blood serum [3], as well as analysis of L-malate content of beverages. In addition, MDH has been used in enzyme-based immunoassays of a wide variety of compounds, particularly abuse drugs used in repetitive therapeutic applications, and hormones.