cellulase has been researched along with titanium-dioxide* in 5 studies
5 other study(ies) available for cellulase and titanium-dioxide
Article | Year |
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Catalytic conversion of sugarcane bagasse to cellulosic ethanol: TiO2 coupled nanocellulose as an effective hydrolysis enhancer.
The present study deals with the production of cellulosic ethanol from bagasse using the synthesized TiO2 coupled nanocellulose (NC-TiO2) as catalyst. Aspergillus nidulans AJSU04 cellulase was used for the hydrolysis of bagasse. NC-TiO2 at various concentrations was added to bagasse in order to enhance the yield of reducing sugars. Complex interaction between cellulase, bagasse, NC-TiO2 and the reaction environment is thoroughly studied. A mathematical model was developed to describe the hydrolysis reaction. Ethanol production from enzymatically hydrolyzed sugarcane bagasse catalyzed with NC-TiO2 was carried out using Saccharomyces cerevisiae ATCC 20602. The glucose release rates and ethanol concentrations were determined. Ethanol produced was found to be strongly dependent on pretreatment given, hydrolysis and fermentation conditions. The study confirmed the promising accessibility of NC-TiO2, for enhanced glucose production rates and improved ethanol yield. Topics: Aspergillus nidulans; Cellulase; Cellulose; Ethanol; Fermentation; Hydrolysis; Industrial Microbiology; Saccharomyces cerevisiae; Titanium | 2016 |
Synergistic Functions of Enzymes Bound to Semiconducting Layers.
Synthesis and cooperative functions of hybrid materials composed of enzyme and semiconducting layers are described in this chapter. The hybrids were produced via a simple physical interaction between the components, that is, electrostatic interaction in an aqueous solution. To form interstratifying enzymes in the galleries, solution pH, which is a key parameter to decide surface potential, should be adjusted appropriately. In other words, enzymes should have an opposite charge when compared to that of the layers at an identical pH. Even though the intercalation slightly reduced enzymatic activity as compared to those of the free enzymes, stability under cruel conditions was drastically improved due to screening effect of semiconducting layers from extrinsic stimuli. In addition, photochemical control of redox enzymes sandwiched between semiconducting layers was accomplished. Light irradiation of the hybrids induced band gap excitation of the layers, and holes produced in the valence band activated the enzymes. It was revealed that the semiconducting layers with magnetic elements might be useful to magnetic application (separation) of enzymes as similar to conventional magnetic beads. Topics: Cellulase; Colloids; Enzymes, Immobilized; Horseradish Peroxidase; Hydrogen-Ion Concentration; Iron; Metal Nanoparticles; Oxidation-Reduction; Particle Size; Potassium; Semiconductors; Solutions; Titanium | 2016 |
Immobilization of cellulase on TiO2 nanoparticles by physical and covalent methods: a comparative study.
Immobilization of cellulase from Aspergillus niger on TiO2 nanoparticles was studied by two different approaches--physical adsorption and covalent coupling. A. niger was selected, as it is generally non-pathogenic, is found in nature in the broad range of habitats and produces cellulase extracellulary. For covalent method, TiO2 nanoparticles were modified with aminopropyltriethoxysilane (APTS). The adsorbed and covalently immobilized enzymes showed 76% and 93% activity, respectively, as compared to the free enzyme. The catalytic efficiency V(max)/K(m) increased from 0.4 to 4.0 after covalent attachment, whereas in adsorption method, it increased slightly from 0.4 to 1.2. The covalently-immobilized and adsorbed cellulase lost only 25% and 50% of their activity, respectively after 60 min of incubation at 75 degrees C. The reusability and operational stability data also showed that covalent coupling increased the stability of the enzyme. The presence of enzyme on TiO2 nanoparticles was confirmed by Fourier-transform infrared spectroscopy. The high-resolution transmission electron microscopy (HR-TEM) and atomic force microscopy (AFM) studies indicated aggregation of enzyme when adsorbed on TiO2 surface and a monolayer of enzyme in covalent attachment. In conclusion, covalently attached cellulase retained good activity and thermal stability, as compared to physically adsorbed enzyme. The lower amount of enzyme activity and thermal stability in case of physically adsorbed immobilized enzyme was due to aggregation of the enzyme after adsorption on TiO2 nanoparticles, as revealed by HR-TEM and AFM. Thus, TiO2 nanoparticles could be suitable candidates for immobilization of cellulase for industrial applications like paper, textile, detergent and food industries. Topics: Aspergillus niger; Cellulase; Enzyme Stability; Enzymes, Immobilized; Kinetics; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Spectroscopy, Fourier Transform Infrared; Titanium | 2014 |
Enhancement of enzymatic hydrolysis and Klason lignin removal of corn stover using photocatalyst-assisted ammonia pretreatment.
Photocatalyst-assisted ammonia pretreatment was explored to improve lignin removal of the lignocellulosic biomass for effective sugar conversion. Corn stover was treated with 5.0-12.5 wt.% ammonium hydroxide, two different photocatalysts (TiO(2) and ZnO) in the presence of molecular oxygen in a batch reactor at 60 °C. Various solid-to-liquid ratios (1:20-1:50) were also tested. Ammonia pretreatment assisted by TiO(2)-catalyzed photo-degradation removed 70 % of Klason lignin under the optimum condition (12.5 % ammonium hydroxide, 60 °C, 24 h, solid/liquid=1:20, photocatalyst/biomass=1:10 with oxygen atmosphere). The enzymatic digestibilities of pretreated corn stover were 85 % for glucan and 75 % for xylan with NH(3)-TiO(2)-treated solid and 82 % for glucan and 77 % for xylan with NH(3)-ZnO-treated solid with 15 filter paper units/g-glucan of cellulase and 30 cellobiase units/g-glucan of β-glucosidase, a 2-13 % improvement over ammonia pretreatment alone. Topics: Ammonium Hydroxide; beta-Glucosidase; Biocatalysis; Biomass; Bioreactors; Cellulase; Fermentation; Hydrolysis; Hydroxides; Lignin; Oxygen; Photolysis; Plant Components, Aerial; Titanium; Zea mays; Zinc Oxide | 2013 |
Enzymes (beta-glucanase and arabinoxylanase) and/or sepiolite supplementation and the nutritive value of maize-barley-wheat based diets for broiler chickens.
1. Two experiments were conducted to study the effects of crude enzyme preparations (beta-glucanase and arabinoxylanase) and/or 20 g/kg Sepiolite (Exal) on the performance and nutrient digestion of broiler chickens fed on maize-barley-wheat based diets. 2. In experiment 1, enzymes improved daily bodyweight gain (by 14%; P<0.001) and food:gain ratios (8%; P<0.001). Sepiolite improved bodyweight gain on the diets not supplemented simultaneously with enzymes (by 6% in 21-d-old chickens, P<0.05) but reduced it for enzymes-supplemeented diets. Changes in productive perfiormance with both additives were associated with changes in diet digestibility and nitrogen balance. 3. In experiment 2, enzyme supplementation reduced viscosity in jejunum and ileum and the mean retention time of digesta in the gut. Sepiolite inclusion significantly reduced the viscosity of jejunum digesta and modified the retention times of digesta in the gut, depending upon whether enzymes had been added. There was a decreased retention time without enzymes but an increase with enzyme supplementation. 4. Although different mechanisms are presumed for enzymes and sepiolite, both seem to counteract the negative effects of soluble, non-starch polysaccharides (NSP) in the diet by modifying jejunal viscosity and improving organic matter digestibility. Topics: Animal Feed; Animals; Antacids; Body Weight; Cellulase; Chickens; Dietary Supplements; Eating; Edible Grain; Feces; Kinetics; Magnesium Silicates; Male; Nutritive Value; Random Allocation; Titanium; Xylosidases | 2000 |