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Literature summary for 3.1.1.11 extracted from

  • de los Santos, M.; Jacobi, S.; Miñarro, M.; Balsalobre, J.; Guillén, A.; Gorbe, M.
    Kinetic characterization, thermal and pH inactivation study of peroxidase and pectin methylesterase from tomato (Solanum betaceum) (2020), Food Sci. Technol., 40, 273-279 .
No PubMed abstract available

Application

Application Comment Organism
food industry study of kinetic characterization, thermal stability and synergistic effect of temperature and pH for peroxidase (POD) and pectin methylesterase (PME) in tomato puree. Inactivation of both enzymes is very important, since these enzymes can have very negative effects on the color, odor, flavor and texture of juices and vegetable beverages during storage. The browning and loss of stability in juices and vegetable beverages, such as tomato puree, can be controlled by applying temperature and pH combinations capable of inactivating these enzymes in a total or partial way, but while respecting the limits organoleptic and legal for juices and vegetable beverages Solanum betaceum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.54
-
Pectin 25°C, pH 7.5 Solanum betaceum

Organism

Organism UniProt Comment Textmining
Solanum betaceum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pectin + n H2O
-
Solanum betaceum n methanol + pectate
-
?

Synonyms

Synonyms Comment Organism
pectin methylesterase
-
Solanum betaceum
PME
-
Solanum betaceum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
5 min, 45% loss of activity Solanum betaceum
90
-
temperature required for total inactivation Solanum betaceum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Solanum betaceum

pH Range

pH Minimum pH Maximum Comment Organism
7 8 pH 7.0: about 35% of maximal activity, pH 8.0: about 25% of maximal activity Solanum betaceum