Influence of Different Lignocellulose Sources on Endo- 1,4-β-Glucanase Gene Expression and Enzymatic Activity of Bacillus amyloliquefaciens B31C
نویسندگان
چکیده
Conversion of cellulose into fermentable sugars for ethanol production is currently performed by enzymatic hydrolysis catalyzed by cellulases. The cellulases are produced by a wide variety of microorganisms, playing a major role in the recycling of biomass. The endo-1,4-β-glucanase (CelB31C) from Bacillus amyloliquefaciens B31C, isolated from compost and previously selected on the basis of highest cellulase activity levels among Bacillus isolated, was characterized as being a potential candidate for a biocatalyst in lignocellulose conversion for secondgeneration bioethanol production. The aim of this work was to evaluate the changes in production of enzymatic activity of the endo-1,4-βglucanase (CelB31C) and the expression of its gene (bglC) using a carboxymethylcellulase activity assay and qRT-PCR analysis, respectively, during growth of B. amyloliquefaciens B31C on different cellulose sources: carboxymethylcellulose (CMC), pure cellulose from Arundo donax, pretreated Arundo donax biomass (Chemtex), and microcrystalline cellulose (Avicel). The results showed that both the expression of bglC gene and the enzymatic activity production are related to the type of cellulose source. The strain showed a high enzymatic activity on lignocellulosic biomass and on microcrystalline cellulose. Furthermore, the highest gene expression occurred during the exponential phase of growth, except in the presence of Avicel.
منابع مشابه
Expression of an Endo-β-1,4-glucanase Gene from Orpinomyces PC-2 in Pichia pastoris
The endo-β-1,4-glucanase gene celE from the anaerobic fungus Orpinomyces PC-2 was placed under the control of an alcohol oxidase promoter (AOX1) in the plasmid pPIC9K, and integrated into the genome of a methylotrophic yeast P. pastoris GS115 by electroporation. The strain with highest endo-β-1,4-glucanase activity was selected and designed as P. pastoris egE, and cultivated in shaking flasks. ...
متن کاملMolecular Cloning, Expression, and Sequence Analysis of Genes Encoding a Xylanase and an Endo-r-(1,3)-(1,4)-Glucanase
endo-beta-(1,3)-(1,4)-glucanase. encoding a xylanase and an expression, and sequence analysis of genes Bacillus polymyxa: molecular cloning, Two beta-glycanase genes are clustered in
متن کاملLignocellulose binding of a Cel5A-RtCBM11 chimera with enhanced β-glucanase activity monitored by electron paramagnetic resonance
Background The Bacillus subtilis endo-β-1,4-glucanase (BsCel5A) hydrolyzes β-1,3-1,4-linked glucan, and the enzyme includes a family 3 carbohydrate-binding module (CBM3) that binds β-1,4-linked glucan. Methods Here we investigate the BsCel5A β-1,3-1,4 glucanase activity after exchanging the CBM3 domain for the family 11 CBM from Ruminiclostridium thermocellum celH (RtCBM11) having β-1,3-1,4 g...
متن کاملProduction and biochemical characterization of a thermostable phytase from Bacillus amyloliquefaciens LOR10
Phytase can improve the nutritional value of plant-based foods by enhancing protein digestibility and mineral availability through phytate digestion in the stomach and the food processing industry. Microbial sources are more promising for the production of phytases on a commercial scale. The objectives of this exploration were to screening and isolation of phytase-producing bacteria from hot sp...
متن کاملCloning and expression of an endo-1,3-1,4-beta-glucanase gene from Bacillus macerans in Lactobacillus reuteri.
Strains of the gastrointestinal species Lactobacillus reuteri were electrotransformed with plasmid constructs containing the endo-1,3-1,4-beta-glucanase gene (bglM) of Bacillus macerans. The enzyme was expressed and secreted by the lactobacilli. A plasmid construct containing the bglM gene lacking its promoter was derived and was demonstrated to be useful as a promoter probe vector.
متن کامل