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Literature summary for 1.14.18.1 extracted from

  • Cabanes, J.; Escribano, J.; Gandia-Herrero, F.; Garcia-Carmona, F.; Jimenez-Atienzar, M.
    Partial purification of latent polyphenol oxidase from peach (Prunus persica L. Cv. Catherina). Molecular properties and kinetic characterization of soluble and membrane-bound forms (2007), J. Agric. Food Chem., 55, 10446-10451.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
SDS soluble and membrane-bound peach polyphenol oxidase are activated by acid shock and the detergent SDS Prunus persica

Application

Application Comment Organism
food industry PPO is a very important enzyme in the food industry because during the processing of fruits and vegetables any wounding may cause cell disruption and lead to the formation of quinones, and their interaction with amino acids and proteins will enhance the brown color produced Prunus persica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.263
-
4-tert-butylcatechol soluble (PPO-S) peach polyphenol oxidase without SDS Prunus persica
0.3
-
4-tert-butylcatechol membrane-bound (PPO-B) peach polyphenol oxidase without SDS Prunus persica
0.85
-
4-tert-butylcatechol membrane-bound (PPO-B) peach polyphenol oxidase with 2 mM SDS Prunus persica
1.84
-
4-tert-butylcatechol soluble (PPO-S) peach polyphenol oxidase with 2 mM SDS Prunus persica

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Prunus persica 16020
-
soluble
-
Prunus persica
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
a partially denaturing SDS-PAGE reveals two very close bands of activity in both cases, but the Western blot performed on a totally denaturing SDS-PAGE, using polyclonal antibodies against bean PPO, reveals a single band in the membrane-bound fraction with a molecular mass of 60 kDa Prunus persica

Organism

Organism UniProt Comment Textmining
Prunus persica
-
Prunus persica L. Cv. Catherina
-

Purification (Commentary)

Purification (Comment) Organism
partial purification, the membrane-bound PPO is extracted by solubilization with the detergent Triton X-114 followed by temperature-induced phase separation Prunus persica

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
Prunus persica
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.063
-
PPO-s soluble, crude extract Prunus persica
0.079
-
PPO-s soluble, supernatant 120000g Prunus persica
0.096
-
PPO-B membrane bound, 6% Triton-X-114 Prunus persica
0.22
-
PPO-B membrane bound, ammoniun sulfate 25-80% Prunus persica
0.45
-
PPO-s soluble, ammoniun sulfate 25-80% Prunus persica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-tert-butylcatechol + 1/2 O2
-
Prunus persica 4-(tert-butyl)benzo-1,2-quinone + H2O
-
?

Synonyms

Synonyms Comment Organism
monophenol, o-diphenol: oxygen oxidoreductase
-
Prunus persica
polyphenol oxidase
-
Prunus persica
PPO
-
Prunus persica
tyrosinase
-
Prunus persica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Prunus persica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Prunus persica

pH Range

pH Minimum pH Maximum Comment Organism
3.5 7.5 enzyme activity toward 5 mM 4-tert-butylcatechol is determined in a range of pH from 3.5 to 7.5 Prunus persica

pI Value

Organism Comment pI Value Maximum pI Value
Prunus persica native isoelectric focusing identifies two acid isoforms of pI 5.7 and 5.8 for the soluble form and one isoform with pI 5.7 for the membrane-bound form
-
5.7
Prunus persica native isoelectric focusing identifies two acid isoforms of pI 5.7 and 5.8 for the soluble form and one isoform with pI 5.7 for the membrane-bound form
-
5.8