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Carbon dioxide/methanol conversion cycle based on cascade enzymatic reactions supported on superparamagnetic nanoparticles Anais da ABC (AABC)
MARQUES NETTO,CATERINA G.C.; ANDRADE,LEANDRO H.; TOMA,HENRIQUE E..
ABSTRACT The conversion of carbon dioxide into important industrial feedstock is a subject of growing interest in modern society. A possible way to achieve this goal is by carrying out the CO2/methanol cascade reaction, allowing the recycle of CO2 using either chemical catalysts or enzymes. Efficient and selective reactions can be performed by enzymes; however, due to their low stability, immobilization protocols are required to improve their performance. The cascade reaction to reduce carbon dioxide into methanol has been explored by the authors, using, sequentially, alcohol dehydrogenase (ADH), formaldehyde dehydrogenase (FalDH), and formate dehydrogenase (FDH), powered by NAD+/NADH and glutamate dehydrogenase (GDH) as the co-enzyme regenerating system....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Carbon dioxide; Enzyme cascade-reaction; Methanol production; Superparamagnetic nanoparticles; Enzymatic catalysis.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652018000200593
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Enzymatic reactions involving the heteroatoms from organic substrates Anais da ABC (AABC)
MARQUES NETTO,CATERINA G.C.; PALMEIRA,DAYVSON J.; BRONDANI,PATRÍCIA B.; ANDRADE,LEANDRO H..
ABSTRACT Several enzymatic reactions of heteroatom-containing compounds have been explored as unnatural substrates. Considerable advances related to the search for efficient enzymatic systems able to support a broader substrate scope with high catalytic performance are described in the literature. These reports include mainly native and mutated enzymes and whole cells biocatalysis. Herein, we describe the historical background along with the progress of biocatalyzed reactions involving the heteroatom(S, Se, B, P and Si) from hetero-organic substrates.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Heteroatom; Biocatalysis; Enzymes; Biotransformation..
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652018000200943
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