19 research outputs found
Immobilization of Polyphenol Oxidase from Princess Tree Leaf and its applications in Dye Decolorization
No full textIn this work, Polyphenol oxidase (PPO) enzyme was extracted and partially purified from princess tree leaves (Paulownia tomentosa). Then, it was immobilized on calcium alginate beads. The free and immobilized PPO enzymes were applied for the decolorization of metal complex and acid dyes. The metal complex and acid dyes in water were mixed with free and immobilized princess tree PPO for one hour. The percent of decolorization was determined by using untreated dye mixture. Immobilized PPO from princess tree leaf was considerably more active in decolorzation of the dyes than the free PPO. Our results suggested that the immobilized princess tree PPO could be useful for removing artificial dyes from industrial wastes
The effect of various metals on polyphenol oxidase and peroxidase activities from goosefeet plant (Chenopodium anthelminthicum)
No full textCatalytic Properties and Immobilization Studies of Catalase from Malva sylvestris L.
No full textCatalase was partially purified from Malva sylvestris L. and immobilized onto chitosan. Then, its catalytic properties were investigated. (NH4)2SO4 precipitation and dialysis were performed in the extracted enzyme. Further purification was performed with sephadex G-200 column. Kinetic studies of the purified enzyme activity were measured and characterized. The inhibitory effects of KCN, NaN3, CuSO4, and EDTA on M. sylvestris L. catalase activity were observed except NaCl. Furthermore, M. sylvestris L. catalase was immobilized covalently with glutaraldehyde onto chitosan particles. The pH and temperature optima as well as the changes in the kinetics (Km, Vmax) of the immobilized and free M. sylvestris L. catalase were determined. The Km value for immobilized catalase (23.4 mM) was higher than that of free enzyme (17.6 mM). Optimum temperature was observed higher than that of the free enzyme. The optimum pH was the same for both free and immobilized catalases (pH 7.50). Immobilized catalase showed higher storage and thermal stabilities than free catalases. Free catalase lost all its activity within 60 days whereas immobilized catalase lost 45% of its activity during the same incubation period at 4°C. The remaining immobilized catalase activity was about 70% after 8 cycles of batch operations
Characterization of activated carbon prepared from agricultural waste and its applications for decolorization of textile dyes
No full textThe Enzymatic Decolorization of Textile Dyes by the Immobilized Polyphenol Oxidase from Quince Leaves
No full textWater pollution due to release of industrial wastewater has already become a serious problem in almost every industry using dyes to color its products. In this work, polyphenol oxidase enzyme from quince (Cydonia Oblonga) leaves immobilized on calcium alginate beads was used for the successful and effective decolorization of textile industrial effluent. Polyphenol oxidase (PPO) enzyme was extracted from quince (Cydonia Oblonga) leaves and immobilized on calcium alginate beads. The kinetic properties of free and immobilized PPO were determined. Quince leaf PPO enzyme stability was increased after immobilization. The immobilized and free enzymes were employed for the decolorization of textile dyes. The dye solutions were prepared in the concentration of 100 mg/L in distilled water and incubated with free and immobilized quince (Cydonia Oblonga) leaf PPO for one hour. The percent decolorization was calculated by taking untreated dye solution. Immobilized PPO was significantly more effective in decolorizing the dyes as compared to free enzyme. Our results showed that the immobilized quince leaf PPO enzyme could be efficiently used for the removal of synthetic dyes from industrial effluents
Dye decolorization by Dandelion (Taraxacum officinale) Polyphenol Oxidase immobilized into Alginate Beads
No full textIn this work, Dandelion (Taraxacum officinale) polyphenol oxidase immobilized on calcium alginate beads was used for the successful and effective decolorization of textile industrial effluent. Polyphenol oxidase (PPO) enzyme was extracted from dandelion (Taraxacum officinale) and immobilized on calcium alginate beads. The immobilized and free enzymes were employed for the decolorization of acid and metal complex dyes. Dye solutions of acid and metal complex dyes were prepared in the concentration 100 mg/L in distilled water and incubated with free and immobilized Dandelion PPO for one hour. The percent decolorization was calculated by taking untreated dye solution. Immobilized PPO was significantly more effective in decolorizing of the dyes as compared to free enzyme. Our results showed that the immobilized Dandelion PPO enzyme could be efficiently used for the removal of synthetic dyes from industrial effluents
Bleaching of Cotton/polyamide fabrics with enzymes and peracetic acid
No full textPresently biotechnology plays an important role especially in the field of environmental protection. In the textile industry, enzymes are often used in many technological processes as they are ecological. This study attempted to introduce the bio-processes in the conventional scouring and bleaching preparation of cotton/polyamide (PA) fabric. We investigated the utilization of peracetic acid formed in situ from reaction of tetraacetylethylenediamine with sodium perborate to affecting bleaching process by using lipase, protease, cellulase, pectinase enzymes. Fabric wettability, tensile strength, whiteness index were taken as a measure of the extent of cotton/PA bleaching. The optimized bleaching recipe and processing were compared with conventional process. Results obtained that, cotton/PA fabric bleached with peracetic acid and either lipase, protease, cellulase or pectinase enzyme shows excellent wettability and acceptable whiteness index. The optimum bleaching recipe consists of 20g/L, tetraacetylethylenediamine; 12g/L, sodium perborate; 2g/L, enzymes; and 1g/L non-ionic wetting agent; the treatment was carried out at 60 degrees C for 45min. This bio-process achieved high quality cotton/PA fabric whiteness to the conventional system at much shorter batch times and with significantly reduced fabric strange lost and alkali consumption, which would be beneficial to the textile industry. (c) 2014 Curtin University of Technology and John Wiley & Sons, Ltd
