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- W2149339768 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) (pI 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)." @default.
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- W2149339768 date "1985-05-01" @default.
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- W2149339768 title "Purification and characterization of pectinesterase and polygalacturonase from<i>Trichoderma reesei</i>" @default.
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- W2149339768 doi "https://doi.org/10.1111/j.1574-6968.1985.tb00680.x" @default.
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