Purification and characterization of pectinesterase and polygalacturonase from Trichoderma reesei |
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Authors: | O. Markovi ,A. Slezá rik,I. Labudová |
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Affiliation: | Institute of Chemistry, Slovak Academy of Sciences, 842 38 Bratislava, Czechoslovakia |
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Abstract: | Abstract Exopolygalacturonase, endopolygalacturonase and pectinesterase were separated from culture filtrates of Trichoderma reesei QM9414 by Sephadex chromatography. Exopolygalacturonase was characterized by specific cleavage of pectic acid to form d -galactopyranuronic acid, and by the hydrolysis of oligomers (highest reaction rate at pentamer). Polygalacturonase exhibited 2 pH-optima peaks (at 4.8 and 5.1) and 10 bands with enzyme activity by isoelectric focusing (IEF) (p I 4.6–8.5). Pectinesterase showed a pH-optimum at 7.6, and 6 enzyme-activity bands on an IEF zymogram which seemed identical with those of higher plants (tomato, alfalfa). |
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Keywords: | Trichoderma reesei QM9414 cultivation on pectin pectic enzyme production polygalacturonase and pectinesterase multiple forms |
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