Cellulases find increasing prominence in sustainable production of fuel and feedstock from lignocellulosic biomass. The purification and biochemical characterization of individual components of cellulase complex is important to understand the mechanism of their action for the solubilization of crystalline cellulose. In this study, an extra-cellular endoglucanase isolated from culture filtrate o...

An endoglucanase was isolated from cell walls of Zea mays seedlings. Characterization of the hydrolytic activity of this glucanase using model substrates indicated a high specificity for molecules containing intramolecular (1-->3),(1-->4)-beta-d-glucosyl sequences. Substrates with (1-->4)-beta-glucosyl linkages, such as carboxymethylcellulose and xyloglucan were, degraded to a limited extent by...

Streptomyces misionensis strain PESB-25 was screened and selected for its ability to secrete cellulases. Cells were grown in a liquid medium containing sugarcane bagasse (SCB) as carbon source and corn steep liquor (CSL) as nitrogen source, whose concentrations were optimized using response surface methodology (RSM). A peak of endoglucanase accumulation (1.01 U · mL(-1)) was observed in a mediu...

Improvement of endoglucanase activity was accomplished by utilizing error-prone rolling circle amplification, supplemented with 1.7 mM MnCl2. This procedure generated random mutations in the Bacillus amyloliquefaciens endoglucanase gene with a frequency of 10 mutations per kilobase. Six mutated endoglucanase genes, recovered from six colonies, possessed endoglucanase activity between 2.50- and ...

An extracellular endoglucanase was isolated from the culture liquid of xylanase producing strain Aspergillus niger B03. The enzyme was purified to a homogenous form, using consecutive ultrafiltration, anion exchange chromatography, and gel filtration. Endoglucanase was a monomer protein with a molecular weight of 26,900 Da determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis,...

Recalcitrance of biomass feedstock remains a challenge for microbial conversion of lignocellulose into biofuel and biochemicals. Clostridium cellulosi, one thermophilic bacterial strain dominated in compost, could hydrolyze lignocellulose at elevated temperature by secreting more than 38 glycoside hydrolases belong to 15 different families. Though one multi-modular endoglucanase CcCel9A has bee...

Cellulolytic fungi can easily be screened within 2 d for the production of cellulolytic enzymes by staining with Congo red, or by measuring the amount of reducing sugar (glucose) produced with the dinitrosalicyclic acid reagent method. Endoglucanase activity is visible in carboxymethyl cellulose agar plates after staining with Congo red, and fixing with HCI or NaOH. This method is essentially b...

The eight-stranded (β/α)8 barrel fold known as the Triosephosphate isomerase (TIM) barrel is the most commonly observed fold in enzymes, displaying an eightfold structural symmetry. The sequences and structures of different TIM barrel enzymes suggest that nature exploits the modularity inherent in the eightfold symmetry to generate enzymes with diverse enzymatic activities and, in certain cases...

Soybean (Glycine max) beta-1,3-endoglucanase (EC 3.2. 1.39) is involved in one of the earliest plant-pathogen interactions that may lead to active disease resistance by releasing elicitor-active carbohydrates from the cell walls of fungal pathogens. Ethylene induced beta-1,3-endoglucanase activity to 2- to 3-fold higher levels in cotyledons of soybean seedlings. A specific polyclonal antiserum ...

A cold-active endoglucanase-producing bacterium was isolated from the Beaufort Sea of Arctic Ocean and identified as Pseudoalteromonas sp. ArcC09. Cellulolytic activity ArcC09 reached a maximum 60 U/mg when cultivated in ZoBell medium for 72 h at 15 °C. This purified endoglucanase, with molecular mass 28 kDa, exhibited pH 7.0 55 The endoglucanase 10% 36% its maximal even low temperatures 5 °C °...