Characterization of a thermostable endoglucanase produced by Isoptericola variabilis sp. IDAH9

• Autor(a) principal: Azizi,Maryam
• Data de Publicação: 2015
• Outros Autores: Hemmat,Jafar, Seifati,Seyed Morteza, Torktaz,Ibrahim, Karimi,Soodabeh
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Microbiology
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822015000401225
• topic: carboxymethyl cellulase; endoglucanase; thermophiles; protein structure

Abstract This study aimed to isolate and evaluate the cellulase activity of cellulolytic bacteria in hot springs of Dehloran, Ilam province, Iran. Water and sludge samples were collected from the hot springs and the bacterial enrichment was performed in a medium containing rice barn and carboxymethyl cellulose (CMC). The cultures were incubated at 50 °C in aerobic conditions. The bacteria were isolated on CMC agar (1%) medium. Cellulase assay of the isolates was measured by the evaluation of endoglucanase enzyme activity, which is also called as carboxymethyl cellulase (CMCase). The isolated thermotolerant bacteria were then identified and optimized for the production of CMCase. Moreover, stabilizing elements of the enzyme were identified with in silico approach. The chosen isolate was identified as Isoptericola variabilis sp. IDAH9. The identified strain produced the most thermostable CMCase at a concentration of 5.6 g/L of ammonium sulfate, 9 g/L CMCase or 12 g/L rice bran, 0/6% Tween-80, and 0.2% sucrose. The produced enzyme showed 80% of the residual activity after 1 h of incubation at 65 °C. In silico data indicated that the remaining residual activity was due to the redundant stabilizing elements in the protein structure. Consequently, I. variabilis can be isolated from the extreme environment and has a thermostable endoglucanase which may be used for various applications after studying them.