Studies on the properties of Celluclast/Eudragit L-100 conjugate.
A cellulase from Trichoderma reesei was immobilized on Eudragit L-100, a reversibly soluble polymer depending on the pH of the medium. The solubility of the modified cellulase was studied at different pH values. By changing the pH, the adsorption equilibrium of the derivatized proteins is switched towards the liquid phase, thus making recycling possible. This method allows for improved stability, without major loss of specific activity. The adsorption of cellulase on Eudragit lowers the enthalpy of denaturation, but affects only slightly the denaturation temperature. The use of carbodiimide was ineffective on linking the enzymes covalently to the polymer, since the immobilization process was found to be only mediated by non-covalent forces.
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Centro de Engenharia Biológica-IBQF, Largo do Paço, Universidade do Minho, 4719 Braga, Portugal.
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D000327:Adsorption; D002480:Cellulase / Q000378:metabolism*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D006863:Hydrogen-Ion Concentration; D011109:Polymethacrylic Acids / Q000737:chemistry* / Q000378:metabolism*; D012680:Sensitivity and Specificity; D012995:Solubility; D014242:Trichoderma / Q000201:enzymology
D004800:Enzymes, Immobilized; D011109:Polymethacrylic Acids; C038300:methylmethacrylate-methacrylic acid copolymer; D002480:Cellulase