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Purification and characterization of an endo-polygalacturonase from Verticillium albo-atrum
Journal of Applied Microbiology, 1999A polygalacturonase was isolated from the culture filtrate of the fungal plant pathogen Verticillium albo-atrum and purified 22-fold to homogeneity as judged by SDS-electrophoresis. The enzyme was a basic protein with a molecular weight of 37 kDa, an isoelectric point ≥8·6 and containing 1·7% carbohydrate.
Mahoney, Raymond R., Huang, L.K.
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Current Microbiology, 1996
Fourteen forms of endopolygalacturonases were purified from the culture medium of Sclerotinia sclerotiorum with ion exchange chromatographies. Individual forms differ in their isoelectric point but exhibit similar molecular masses. On the basis of the cross-reactions to antibodies raised against a purified acidic endopolygalacturonase, these forms ...
, Martel, , Letoublon, , Fevre
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Fourteen forms of endopolygalacturonases were purified from the culture medium of Sclerotinia sclerotiorum with ion exchange chromatographies. Individual forms differ in their isoelectric point but exhibit similar molecular masses. On the basis of the cross-reactions to antibodies raised against a purified acidic endopolygalacturonase, these forms ...
, Martel, , Letoublon, , Fevre
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Protein Expression and Purification, 2007
Endo-polygalacturonases (endoPGs) belong to the glycoside hydrolase family 28 and hydrolyze the alpha-1,4 glycosidic bond present in the smooth regions of pectins. Pectic substances are among the principal macromolecular components of the primary plant cell walls and are subjected to enzymatic degradation not only in the course of important ...
Massa C +4 more
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Endo-polygalacturonases (endoPGs) belong to the glycoside hydrolase family 28 and hydrolyze the alpha-1,4 glycosidic bond present in the smooth regions of pectins. Pectic substances are among the principal macromolecular components of the primary plant cell walls and are subjected to enzymatic degradation not only in the course of important ...
Massa C +4 more
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Archives of Biochemistry and Biophysics, 1969
Abstract A polygalacturonase has been purified 239 fold from the culture filtrate of Corticium rolfsii, and found to be a homogeneous protein by ultracentrifugal analysis. The enzyme is typical of an endo-polygalacturonase with a optimum for catalytic activity at pH 2.5.
A, Kaji, T, Okada
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Abstract A polygalacturonase has been purified 239 fold from the culture filtrate of Corticium rolfsii, and found to be a homogeneous protein by ultracentrifugal analysis. The enzyme is typical of an endo-polygalacturonase with a optimum for catalytic activity at pH 2.5.
A, Kaji, T, Okada
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The Chemical Engineering Journal, 1989
Abstract Endo-polygalacturonase can be purified and isolated from an industrial pectolytic enzyme preparation using alginate as an affinity adsorbent in a fluid The adsorption and desorption kinetics of the system have been studied. First the adsorption and desorption conditions were optimized with respect to p The stability of the beads was tested
W. Somers +4 more
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Abstract Endo-polygalacturonase can be purified and isolated from an industrial pectolytic enzyme preparation using alginate as an affinity adsorbent in a fluid The adsorption and desorption kinetics of the system have been studied. First the adsorption and desorption conditions were optimized with respect to p The stability of the beads was tested
W. Somers +4 more
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Purification of endo-polygalacturonase by affinity precipitation using alginate.
Biotechnology and applied biochemistry, 1994The precipitation of alginate by Ca2+ at pH 3.8 was found to occur concomitantly with the precipitation of endo-polygalacturonase from Aspergillus niger. Under optimum conditions, 92% of the enzyme activity was precipitated. The enzyme could be recovered from the precipitate by washing with 0.5 M NaCl/0.2 M Ca2+.
M N, Gupta, G, Dong, B, Mattiasson
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Endo-polygalacturonase from Cladosporium cucumerinum elicits lignification in cucumber hypocotyls
Physiological and Molecular Plant Pathology, 1987Abstract The cucumber pathogen Cladosporium cucumerinum produces one endo-polygalacturonase and at least two exo-polygalacturonases during growth in a liquid medium containing citrus pectin as the carbon source. The endo-polygalacturonase was purified nine-fold by ion-exchange chrumatography and gel filtration.
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Physiological and Molecular Plant Pathology, 1999
Abstract A major endo-polygalacturonase (PG1), produced both in vivo in inoculated potato tubers andin vitro on crude cell walls of Corylus avellana by an isolate of a Zimbabwean species of Armillaria (group III), was purified 18.8-fold, to apparent homogeneity on SDS-PAGE, by gel filtration followed by cation-exchange chromatography.
E. MWENJE, J.P. RIDE
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Abstract A major endo-polygalacturonase (PG1), produced both in vivo in inoculated potato tubers andin vitro on crude cell walls of Corylus avellana by an isolate of a Zimbabwean species of Armillaria (group III), was purified 18.8-fold, to apparent homogeneity on SDS-PAGE, by gel filtration followed by cation-exchange chromatography.
E. MWENJE, J.P. RIDE
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The active site of yeast endo-polygalacturonase contains seven subsites
Phytochemistry, 1979Abstract The rate of hydrolysis of oligomers by the endopolygalacturonase of yeast is in the order: heptamer > hexamer > pentamer > tetramer. This suggests that the active site accommodates at least 7 units. Since the heptamer disappears concurrently with the bulk of larger oligomers, the maximum number of units appears to be 7.
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