Endopolygalacturonase from Fusarium moniliforme was used to degrade acetylated homogalacturonan previously prepared from sugar beet pulp. The initial velocity and the final percentage of hydrolysis decreased-very rapidly with increasing degree of acetylation, showing that acetyl substitution markedly affected the enzymatic activity. MALDI-TOF mass spectrometry was used to analyse the reaction products and to show acetyl groups on the oligogalacturonates. The results demonstrated that the enzyme was able to accommodate acetyl groups in its active site cleft. The influence of acetyl groups on the mode of action of the enzyme was discussed and compared to the influence of methyl groups. (C) 2003 Elsevier Science Ltd. All rights reserved
To assess the subsites involved in substrate binding in Aspergillus niger endopolygalacturonase II, ...
Pure saturated and unsaturated oligogalacturonic acids, including unsaturated monogalacturonic acid,...
Polygalacturonases specifically hydrolyze polygalaturonate, a major constituent of plant cell wall p...
Endopolygalacturonase from Fusarium moniliforme was used to degrade acetylated homogalacturonan prev...
The structures of complexes of Fusarium moniliforme endopolygalacturonase (endoPG) with non-methylat...
International audienceEndopolygalacturonases (EndoPGs) hydrolyse the 1-4 linkages between two -D-gal...
Investigations on the mode of action of Aspergillus niger pectin methylesterase (PME) towards differ...
Studies of the enzymic digestion of pectic substrates using different polygalacturonase (PG) prepara...
A thorough investigation of the mode of action of Aspergillus niger (4M-147) pectin lyase A (PLA) on...
Two monomethyl esters of -(1-4)-linked D-galacturonic dimers and three monomethyl esters of -(1-4)-l...
A method was developed that enabled the study of non-esterified galacturonic acid sequences (so-call...
To reveal the ester distribution patterns in acetylated pectins, an enzymatic fingerprinting method ...
Methyl-esterified and methyl-glycosydated oligogalacturonides (oligoGalA) were produced to be used a...
The substrate specificity and the mode of action of Aspergillus niger pectin methylesterase (PME) wa...
The enzymes pectin methylesterase and polygalacturonate hydrolase, which are responsible for the ini...
To assess the subsites involved in substrate binding in Aspergillus niger endopolygalacturonase II, ...
Pure saturated and unsaturated oligogalacturonic acids, including unsaturated monogalacturonic acid,...
Polygalacturonases specifically hydrolyze polygalaturonate, a major constituent of plant cell wall p...
Endopolygalacturonase from Fusarium moniliforme was used to degrade acetylated homogalacturonan prev...
The structures of complexes of Fusarium moniliforme endopolygalacturonase (endoPG) with non-methylat...
International audienceEndopolygalacturonases (EndoPGs) hydrolyse the 1-4 linkages between two -D-gal...
Investigations on the mode of action of Aspergillus niger pectin methylesterase (PME) towards differ...
Studies of the enzymic digestion of pectic substrates using different polygalacturonase (PG) prepara...
A thorough investigation of the mode of action of Aspergillus niger (4M-147) pectin lyase A (PLA) on...
Two monomethyl esters of -(1-4)-linked D-galacturonic dimers and three monomethyl esters of -(1-4)-l...
A method was developed that enabled the study of non-esterified galacturonic acid sequences (so-call...
To reveal the ester distribution patterns in acetylated pectins, an enzymatic fingerprinting method ...
Methyl-esterified and methyl-glycosydated oligogalacturonides (oligoGalA) were produced to be used a...
The substrate specificity and the mode of action of Aspergillus niger pectin methylesterase (PME) wa...
The enzymes pectin methylesterase and polygalacturonate hydrolase, which are responsible for the ini...
To assess the subsites involved in substrate binding in Aspergillus niger endopolygalacturonase II, ...
Pure saturated and unsaturated oligogalacturonic acids, including unsaturated monogalacturonic acid,...
Polygalacturonases specifically hydrolyze polygalaturonate, a major constituent of plant cell wall p...