Purification and properties of a protein from Lantana camara activating Cuscuta reflexa cellulase
1999
Chatterjee, U. | Sanwal, G.G.
A high molecular weight protein from Lantana camara leaf and petiole was purified 59-fold with 12% recovery by heat treatment, ammonium sulfate fractionation and subsequent chromatography on DEAE-cellulose and Sephadex G-200. It has been designated as cellulase stimulator (C(s)) in view of its ability to stimulate/activate Cuscuta reflexa cellulase catalysis. The purified protein gave a single C(s)-activity and protein peak on chromatography, a single band on PAGE at various pH values and a single peak on FPLC. The purified C(s)-protein alone did not show cellulolytic activity with CM-cellulose but in recombination experiments with C. reflexa CM-cellulase, it exhibited activation effect both in terms of saccharifying and liquefying activity. The purified protein had a molecular mass 230 kDa and Stokes' radius of 62.5 angstrom.
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