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3.2.1.67: galacturonan 1,4-alpha-galacturonidase

This is an abbreviated version!
For detailed information about galacturonan 1,4-alpha-galacturonidase, go to the full flat file.

Word Map on EC 3.2.1.67

Reaction

[(1->4)-alpha-D-galacturonide]n
+
H2O
=
[(1->4)-alpha-D-galacturonide]n-1
 +
D-galacturonate

Synonyms

alkaline exo-polygalacturonase, carrot exopolygalacturonase, CbPelA, corn pollen polygalacturonase, EPG, exo polygalacturonase, exo-D-galacturonanase, exo-D-galacturonase, Exo-PG, exo-PGase, exo-PGI, exo-PGII, exo-PGU B, exo-poly alpha galactouronosidase, exo-polygalacturonanase, exo-polygalacturonase, exolytic PGase, exoPG, exoPG1, exoPG2, exoPGase, exopoly-D-galacturonase, exopolygalacturonanase, exopolygalacturonase, exopolygalacturonase B, exopolygalacturonase X, Galacturan 1,4-alpha-galacturonidase, GH28, macerating enzyme, More, MpPG1, MpPG3, oligogalacturonate hydrolase, peach exopolygalacturonase, PECI, pectinase, PelB, PG III, PGase, PGase I, PGC2, PGC3, PGI, poly 1,4-alpha-D-galacturonide-galacturonohydrolase, Poly(1,4-alpha-D-galacturonide)galacturonohydrolase, poly(galacturonate)hydrolase, poly-(1-4)-alpha-D-galactosiduronate glycanohydrolase, polygalacturonanase, polygalacturonase, polymethylgalacturonase, RPG15, RPG16, SSXPG1, SSXPG2, TM0437, TmGalU, YeGH2

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.67 galacturonan 1,4-alpha-galacturonidase

General Stability

General Stability on EC 3.2.1.67 - galacturonan 1,4-alpha-galacturonidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 mM Ba2+ increases thermal stability by 30%, besides increasing its stability at acid pH
-
anion exchange resins stabilize the enzyme
-
Ca2+ enhances the stability of enzyme and its activity by 30%
-
calcium alginate-immobilized polygalacturonase exhibits more stability to changes in pH than the temperature. The activity of the immobilized polygalacturonase reduces to 34.56% and 14.81% of the initial activity in the second and third catalytic cycles, respectively
-
rather unstable
-
stability studies of the enzyme at different pH values after 24 h of incubation at room temperature give the highest percentage residual activities as follows: 23.01% at pH 4.5 in acetate, 28.32% at pH 7.0 in phosphate, and 22.13% at pH 7.5 in Tris-HCl
-
stable at room temperature for 24 h
-
stable in acidic medium
-
stable, even at high temperatures, relatively stable in acidic and neutral, unstable in alkaline media
-
the affinity of enzyme towards its substrate is reduced after immobilization on sodium-alginate matrix and Vmax of covalently immobilized enzyme decrease to 66.7% while the Vmax value of adsorbed enzyme increase up to 150% as compared to free counterpart
-