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Glucose isomerization in simulated moving bed reactor by Glucose isomerase BABT
Silva,Eduardo Alberto Borges da; Souza,Antônio Augusto Ulson de; Rodrigues,Alírio Egídio; Souza,Selene Maria Arruda Guelli Ulson de.
Studies were carried out on the production of high-fructose syrup by Simulated Moving Bed (SMB) technology. A mathematical model and numerical methodology were used to predict the behavior and performance of the simulated moving bed reactors and to verify some important aspects for application of this technology in the isomerization process. The developed algorithm used the strategy that considered equivalences between simulated moving bed reactors and true moving bed reactors. The kinetic parameters of the enzymatic reaction were obtained experimentally using discontinuous reactors by the Lineweaver-Burk technique. Mass transfer effects in the reaction conversion using the immobilized enzyme glucose isomerase were investigated. In the SMB reactive system,...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Simulated moving bed reactor; Glucose isomerization; Enzymatic kinetics; Mass transfer; Mathematical model; Dynamic simulation.
Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132006000400018
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Purification and characterization of cytosolic and cell wall β-galactosidases from Vigna unguiculata stems Braz. J. Plant Physiol.
Sudério,Fabrício Bonfim; Barbosa,Gislainy Karla da Costa; Gomes-Filho,Enéas; Enéas-Filho,Joaquim.
Three β-galactosidase isoforms, β-gal I and β-gal II (cytosolic) and β-gal III (cell wall-associated), were isolated from stems of Vigna unguiculata (L.) Walp. cv. Pitiúba seedlings. Purification consisted of aμMonia sulfate fractionation followed by chromatography in DEAE-Sephadex and Lactosyl-Sepharose columns. The two cytosolic isoforms showed the same chromatography pattern, which differed from that of β-gal III. Electrophoresis revealed a single band of protein for β-gal II and β-gal III which also expressed β-galactosidase activity in gel. The apparent molecular mass of the β-gal I, II and III was 89, 146 and 124 kDa, respectively. The three isoforms revealed the same optimal pH (4.0) and the same optimal assay temperature (55ºC) for enzyme activity....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Enzymatic kinetics; Cowpea; Optimal pH; Enzyme purification; Thermal stability; Thermal inactivation.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202011000100003
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