Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados Electron. J. Biotechnol. (3) BJM (1) Autor Ibrahim,Abdelnasser S.S. (4) Al-Salamah,Ali A (2) El-Tayeb,Mohamed A (2) El-Toni,Ahmed Mohamed (2) Elbadawi,Yahya B (2) Al-Salamah,Ali A. (1) Al-Sharawi,Samar Z.R. (1) Almaary,Khalid S. (1) El-Shatoury,Einas H (1) El-Tayeb,Mohamed A. (1) Elbadawi,Yahya B. (1) Eldiwany,Ahmad (1) Gebreel,Hassan M (1) Mais... Palavra-chave Amphibacillus sp (2) Cyclodextrin glucanotransferase (2) Cyclodextrins (2) Immobilization (2) Amphibacillus sp. NPST-10 (1) Antibiotic resistance (1) Antimicrobials resistance determinants (1) Cyclodextrin glycosyltransferase (1) Double mesoporous core-shell silica nanospheres (1) Magnetic nanoparticle (1) Salmonella (1) Serotyping (1) Silica (1) Wadi Natrun soda lakes (1) Mais... Tipo do documento Journal article (3) Info:eu-repo/semantics/article (1) Ano 2017 (1) 2014 (1) 2013 (2) País Chile (3) Brazil (1) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última A new low molecular mass alkaline cyclodextrin glucanotransferase from Amphibacillus sp. NRC-WN isolated from an Egyptian soda lake Electron. J. Biotechnol. Al-Sharawi,Samar Z.R.; Ibrahim,Abdelnasser S.S.; El-Shatoury,Einas H; Gebreel,Hassan M; Eldiwany,Ahmad. Background: Cyclodextrin glucanotransferase (CGTase) is one of the most industrially important enzymes used in the commercial production of cyclodextrins (CDs). Alkaliphilic bacteria have attracted much interest in the last few decades because of their ability to produce extracellular enzymes that are active and stable at high pH values. Here, we report the isolation of a new CGTase from alkaliphilic bacteria collected from Egyptian soda lakes and describe the purification and biochemical characterization of this CGTase. Results: Screening for CGTase-producing alkaliphilic bacteria from sediment and water samples collected from Egyptian soda lakes located in the Wadi Natrun valley resulted in the isolation of a potent CGTase-producing alkaliphilic... Tipo: Journal article Palavras-chave: Amphibacillus sp; Cyclodextrin glycosyltransferase; Cyclodextrins; Wadi Natrun soda lakes. Ano: 2013 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000600003 Cyclodextrin glucanotransferase immobilization onto functionalized magnetic double mesoporous core-shell silica nanospheres Electron. J. Biotechnol. Ibrahim,Abdelnasser S.S.; Al-Salamah,Ali A; El-Toni,Ahmed Mohamed; El-Tayeb,Mohamed A; Elbadawi,Yahya B. Background Cyclodextrin glucanotransferase (CGTase) from Amphibacillus sp. NPST-10 was covalently immobilized onto amino-functionalized magnetic double mesoporous core-shell silica nanospheres (mag@d-SiO2@m-SiO2-NH2), and the properties of the immobilized enzyme were investigated. The synthesis process of the nanospheres included preparing core magnetic magnetite (Fe3O4) nanoparticles, coating the Fe3O4 with a dense silica layer, followed by further coating with functionalized or non-functionalized mesoporous silica shell. The structure of the synthesized nanospheres was characterized using TEM, XRD, and FT-IR analyses. CGTase was immobilized onto the functionalized and non-functionalized nanospheres by covalent attachment and physical adsorption. Results... Tipo: Journal article Palavras-chave: Amphibacillus sp; Cyclodextrin glucanotransferase; Cyclodextrins; Double mesoporous core-shell silica nanospheres; Immobilization. Ano: 2014 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000200001 Immobilization of cyclodextrin glucanotransferase on aminopropyl-functionalized silica-coated superparamagnetic nanoparticles Electron. J. Biotechnol. Ibrahim,Abdelnasser S.S.; Al-Salamah,Ali A; El-Toni,Ahmed Mohamed; El-Tayeb,Mohamed A; Elbadawi,Yahya B. Background: Cyclodextrin glycosyltransferase (CGTase) from Amphibacillus sp. NPST-10 was successfully covalently immobilized on aminopropyl-functionalized silica coated superparamagnetic nanoparticles; and the properties of immobilized enzyme were investigated. The synthesis process included preparing of core magnetic magnetite (Fe3O4) nanoparticles using solvothermal synthesis; followed by coating of Fe3O4 nanoparticles with dense amino-functionalized silica (NH2-SiO2) layer using in situ functionalization method. The structure of synthesized Fe3O4@NH2-SiO2 nanoparticles was characterized using TEM, XRD, and FT-IR analysis. Fe3O4@NH2-SiO2 nanoparticles were further activated by gluteraaldehyde as bifunctional cross linker, and the activated nanoparticles... Tipo: Journal article Palavras-chave: Amphibacillus sp. NPST-10; Cyclodextrin glucanotransferase; Immobilization; Magnetic nanoparticle; Silica. Ano: 2013 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000600010 Prevalence, serotyping and antimicrobials resistance mechanism of Salmonella enterica isolated from clinical and environmental samples in Saudi Arabia BJM El-Tayeb,Mohamed A.; Ibrahim,Abdelnasser S.S.; Al-Salamah,Ali A.; Almaary,Khalid S.; Elbadawi,Yahya B.. Abstract Salmonella is recognized as a common foodborne pathogen, causing major health problems in Saudi Arabia. Herein, we report epidemiology, antimicrobial susceptibility and the genetic basis of resistance among S. enterica strains isolated in Saudi Arabia. Isolation of Salmonella spp. from clinical and environmental samples resulted in isolation of 33 strains identified as S. enterica based on their biochemical characteristics and 16S-rDNA sequences. S. enterica serovar Enteritidis showed highest prevalence (39.4%), followed by S. Paratyphi (21.2%), S. Typhimurium (15.2%), S. Typhi and S. Arizona (12.1%), respectively. Most isolates were resistant to 1st and 2nd generation cephalosporin; and aminoglycosides. Moreover, several S. enterica isolates... Tipo: Info:eu-repo/semantics/article Palavras-chave: Salmonella; Serotyping; Antibiotic resistance; Antimicrobials resistance determinants. Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822017000300499 Registros recuperados: 4 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