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Medium initial pH and carbon source stimulate differential alkaline cellulase time course production in Stachybotrys microspora.
Ben Hmad, Ines; Abdeljalil, Salma; Saibi, Walid; Amouri, Bahia; Gargouri, Ali.
Afiliação
  • Ben Hmad I; Laboratory of Biomass Valorisation and Protein Production in Eucaryotes, Centre of Biotechnology of Sfax (CBS)/University of Sfax, B.P "1177", 3018, Sfax, Tunisia.
Appl Biochem Biotechnol ; 172(5): 2640-9, 2014 Mar.
Article em En | MEDLINE | ID: mdl-24420284
ABSTRACT
The production profile of cellulases of the mutant strain A19 from the filamentous fungus Stachybotrys microspora was studied in the presence of various carbon sources (glucose, lactose, cellulose, carboxymethylcellulose (CMC), and wheat bran) and a range of medium initial pH (5, 7, and 8). Two extracellular cellulases from the Stachybotrys strain (endoglucanases and ß-glucosidases) were monitored by enzymatic assay, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and zymogram analysis. Glucose and lactose repressed CMCase time course production while they permitted a strong ß-glucosidase one. On Avicel cellulose, CMC, and wheat bran, both activities were highly produced. Wheat bran (WB) is the best carbon source with an optimum of production at days 5 and 6. The production kinetics of both activities were shown to depend on the medium initial pH, with a preference for neutral or alkaline pH in the majority of conditions. The exception concerned the ß-glucosidase which was much more produced at acidic pH, on glucose and cellulose. Most interestingly, a constitutive and conditional expression of an alkaline endoglucanase was revealed on the glucose-based medium at an initial pH of 8 units. The zymogram analysis confirmed such conclusions and highlighted that carbon sources and the pH of the culture medium directed a differential induction of various endoglucanases and ß-glucosidases.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Stachybotrys / Proteínas Fúngicas / Celulases Idioma: En Revista: Appl Biochem Biotechnol Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Tunísia

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Stachybotrys / Proteínas Fúngicas / Celulases Idioma: En Revista: Appl Biochem Biotechnol Ano de publicação: 2014 Tipo de documento: Article País de afiliação: Tunísia