Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados BABT (1) Electron. J. Biotechnol. (1) Autor Araújo,Heloísa Sobreiro Selistre (1) Giordano,Raquel de Lima Camargo (1) González,José Miguel (1) Gómez,José Manuel (1) Illanes,Andrés (1) Pinotti,Laura Marina (1) Silva,Ana C. G. (1) Souza,Vanessa Ribeiro de (1) Valencia,Pedro (1) Wilson,Lorena (1) Mais... Palavra-chave Penicillin G acylase (2) Bacillus megaterium (1) Characterization (1) Diffusional restrictions (1) Enzyme kinetics (1) Immobilized enzyme (1) Penicillin hydrolysis (1) Mais... Tipo do documento Info:eu-repo/semantics/article (1) Journal article (1) Ano 2010 (1) 2005 (1) País Brazil (1) Chile (1) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Diffusional restrictions in glyoxyl-agarose immobilized penicillin G acylase of different particle size and protein loading Electron. J. Biotechnol. Illanes,Andrés; González,José Miguel; Gómez,José Manuel; Valencia,Pedro; Wilson,Lorena. Particle size and enzyme protein loading are design parameters of enzyme immobilization affecting biocatalyst performance that can be varied within broad margins. Their effect on mass transfer limitations at different bulk penicillin G concentrations has been studied with glyoxyl agarose immobilized penicillin G acylase biocatalysts of average particle size of 5·10-5m and 10·10-4m at protein loadings from 15 to 130 mg/g gel. Internal diffusional restrictions were evaluated for such biocatalysts: Thiele modulus varied from 1.17 for the small particles at the lower protein load to 5.84 for the large particles at the higher protein load. Effectiveness factors at different bulk substrate concentrations were determined for all biocatalysts, values ranging from... Tipo: Journal article Palavras-chave: Diffusional restrictions; Enzyme kinetics; Immobilized enzyme; Penicillin G acylase; Penicillin hydrolysis. Ano: 2010 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000100002 Characterization of the penicillin G acylase from Bacillus megaterium ATCC 14945 BABT Souza,Vanessa Ribeiro de; Silva,Ana C. G.; Pinotti,Laura Marina; Araújo,Heloísa Sobreiro Selistre; Giordano,Raquel de Lima Camargo. The purpose of this work was to characterize the enzyme penicillin G acylase (PGA) produced by Bacillus megaterium. Purification of the enzyme by ultra/diafiltration did not allow the detection of the PGA band by SDS-PAGE electrophoresis due to the high content of remaining proteins. However, using the DNA of the microorganism, it was possible to replicate the genes of the two B. megaterium PGA reported in literature, showing that the enzyme consisted of two sub-units, having 245 and 537 amino acids each and an average molecular mass of 26950 and 59070 Da, respectively. The parameters studied were: 1) the influence of temperature in the 25-60(0)C range, 2) pH in the 5-10 range and 3) substrate concentration, this was tested to obtain results on the... Tipo: Info:eu-repo/semantics/article Palavras-chave: Penicillin G acylase; Bacillus megaterium; Characterization. Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132005000400013 Registros recuperados: 2 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco