Open AccessPurification and characterization of pectinesterase and polygalacturonase from Trichoderma reesei
Author(s) -
Markovič O.,
Slezárik A.,
Labudová I.
Publication year - 1985
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1985.tb00680.x
Subject(s) - trichoderma reesei , pectinesterase , pectinase , chemistry , isoelectric focusing , hydrolysis , chromatography , biochemistry , zymography , isoelectric point , sephadex , enzyme , cellulase
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).