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    The effect of pH on the foam fractionation of ß-glucosidase and cellulase

    Year: 2003

    Journal: -, 20111221

    Authors: William D. Lambert , Liping Du , Yufeng Ma , Veara Loha , Vorakan Burapatana , Ales Prokop , Robert D. Tanner *, Neville B. Pamment

    Organizations: a Department of Chemical Engineering, Vanderbilt University, Nashville, TN 37235, USA b Department of Chemistry, Vanderbilt University, Nashville, TN 37235, USA c Department of Chemical Engineering, King Mongkut's Institute of Technology Thonburi, Bangkok 10140, Thailand d Department of Chemical Engineering, University of Melbourne, Parkville, Victoria 3052, Australia

    The surface tension-pH profile of ß-glucosidase was established to determine its relationship to the corresponding profile of cellulase and to the foam fractionation of that cellulase. The goal of this work was to determine the optimal foaming points for both cellulase and cellobiase. This data may prove useful in the separation of certain components of cellulase, since the non-foaming hydrophilic ß-glucosidase does not foam as well as the hydrophobic components of cellulase at low concentrations. A key finding from these experiments was that there are two local minima in the surface tension-pH trajectory for Trichoderma reesei cellulase, as contrasted to the usual single minimum. The lower of these minimum points corresponds to the cellulase isoelectric point. The double minimum surface tension-pH profile was also observed for cellobiase alone. The optimal foaming pH for cellobiase alone was determined to be around 10.5, while for cellulase it was between 6 and 9.