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	Provedor de dados BABT (1) BJM (1) Autor Aygan,Ashabil (2) Altun,Hanifi (1) Arikan,Burhan (1) Comlekcioglu,Ugur (1) Dinçer,Sadik (1) Ekiz,Dilek Ozgun (1) Gunes,Merva (1) Korkmaz,Hatice (1) Çolak,Ömer (1) Mais... Palavra-chave Alkaliphilic (1) Bacillus sp. (1) Cellulase (1) Coexpression (1) E. coli (1) Enzyme (1) Rumen fungi (1) Thermostable (1) Xylanase (1) Α-amylase (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2017 (1) 2008 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli BABT Comlekcioglu,Ugur; Gunes,Merva; Altun,Hanifi; Ekiz,Dilek Ozgun; Aygan,Ashabil. ABSTRACT Rumen fungi inhabit the gastro-intestinal tract of ruminants and the most non-ruminant herbivores. Rumen fungi produce highly active plant cell wall degrading enzymes, therefore they have gained scientific interest. In this study, genes encoding xylanase (xynA-7) and cellulase (celA-5) were amplified from Neocallimastix sp. GMLF7 and Orpinomyces sp. GMLF5, respectively, and expressed in Escherichia coli. XynA-7 was found to be active only on xylan, however CelA-5 had activity both on carboxymethyl cellulose and lichenan. Lichenase activity of CelA-5 was found to be higher than carboxymethyl cellulase activity. The optimal conditions were at pH 6.0 and 40 °C for CelA-5 and at pH 6.5 and 50 °C for XynA-7. A coexpression vector was constructed to... Tipo: Info:eu-repo/semantics/article Palavras-chave: Rumen fungi; Xylanase; Cellulase; Coexpression; E. coli. Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132017000100407 Highly thermostable and alkaline α-amylase from a halotolerant-alkaliphilic Bacillus sp. AB68 BJM Aygan,Ashabil; Arikan,Burhan; Korkmaz,Hatice; Dinçer,Sadik; Çolak,Ömer. An alkaliphilic and highly thermostable α-amylase producing Bacillus sp. was isolated from Van soda lake. Enzyme synthesis occurred at temperatures between 25ºC and 40ºC. Analysis of the enzyme by SDS-PAGE revealed a single band which was estimated to be 66 kDa. The enzyme was active in a broad temperature range, between 20ºC and 90ºC, with an optimum at 50ºC; and maximum activity was at pH 10.5. The enzyme was almost completely stable up to 80ºC with a remaining activity over 90% after 30 min pre-incubation. Thermostability was not increased in the presence of Ca2+. An average of 75% and 60ºC of remaining activity was observed when the enzyme was incubated between pH 5 and 9 for 1 h and for 2 h, respectively. The activity of the enzyme was inhibited by... Tipo: Info:eu-repo/semantics/article Palavras-chave: Bacillus sp.; Α-amylase; Alkaliphilic; Thermostable; Enzyme. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000300027 Registros recuperados: 2 Primeira ... 1 ... Última

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