Preparation and properties of pectic enzymes produced by Trichoderma lignorum.
Polygalacturonase and protein-methylesterase were isolated from shaken culture of Trichoderma lignorium. Isolation was carried out with various agents. Methanol was the most suitable precipitant for isolating polygalacturonase, yielding enzyme preparations 6.6 times more active than that of culture filtrate. Likewise, tannin afforded active fractions at pH 4 and 0.05% concentrations. Similarly, 50% ammonium sulphate saturation gave active fractions. The least polygalacturonase activity was obtained from ethanol. In any of the organic solvents used, highest enzymic activity was obtained when using only one volume. As regards pectin-methylesterase, no correlation existed between its activity and concentration of the precipitant used. A substrate concentration above 0.8% was a limiting factor for polygalacturonase activity, while optimum enzyme concentration was 40 microgram protein/ml at 40 degrees C and pH 4.45.
D004950:Esterases / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D003904:Mitosporic Fungi / Q000201:enzymology*; D010368:Pectins / Q000378:metabolism; D011096:Polygalacturonase / Q000378:metabolism*; D014242:Trichoderma / Q000201:enzymology*; D014783:Viscosity
D010368:Pectins; D004950:Esterases; D006026:Glycoside Hydrolases; D011096:Polygalacturonase