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Literature summary for 1.14.18.1 extracted from

  • Zhu, Z.; Zhan, L.
    Characterization of polyphenol oxidase from water caltrop (Trapa acornis Nakano) fruits (2010), J. Food Biochem., 34, 1125-1140.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
CaCl2 373.5% relative activity at 5 mM Trapa acornis
MnSO4 488.1% relative activity at 10 mM Trapa acornis
SDS 342.4% relative activity at 10 mM Trapa acornis
Triton X-100 121% relative activity at 5 mM Trapa acornis

Inhibitors

Inhibitors Comment Organism Structure
ascorbic acid 17.6% residual activity at 1 mM Trapa acornis
Citric acid 26% residual activity at 1 mM Trapa acornis
EDTA 53.3% residual activity at 0.5 mM Trapa acornis
L-cysteine 10.8% residual activity at 0.5 mM Trapa acornis
NaCl 39.6% residual activity at 0.5 mM Trapa acornis
reduced glutathione 42% residual activity at 1 mM Trapa acornis
Thiourea 9.6% residual activity at 1 mM Trapa acornis
Triton X-100 42.5% residual activity at 10 mM Trapa acornis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
15.4
-
catechol at pH 6.0, 20°C Trapa acornis
21.2
-
gallic acid at pH 7.0, 30°C Trapa acornis
57
-
pyrogallol at pH 7.0, 30°C Trapa acornis
77
-
L-tyrosine at pH 5.8, 30°C Trapa acornis
129.5
-
chlorogenic acid at pH 7.0, 30°C Trapa acornis
174.5
-
caffeic acid at pH 6.0, 20°C Trapa acornis

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Trapa acornis 9507
-

Organism

Organism UniProt Comment Textmining
Trapa acornis
-
water caltrop
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation Trapa acornis

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
Trapa acornis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 catechol + O2 most suitable substrate Trapa acornis 2 1,2-benzoquinone + 2 H2O
-
?
caffeic acid + O2 31% activity at 2.5 mM substrate concentration Trapa acornis caffeoyl quinone + H2O
-
?
chlorogenic acid + O2
-
Trapa acornis ?
-
?
gallic acid + O2 39% activity at 2.5 mM substrate concentration Trapa acornis ?
-
?
L-tyrosine + O2
-
Trapa acornis L-DOPA + H2O
-
?
pyrogallol + O2
-
Trapa acornis ?
-
?

Synonyms

Synonyms Comment Organism
polyphenol oxidase
-
Trapa acornis
PPO
-
Trapa acornis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
for catechol and caffeic acid Trapa acornis
30
-
for gallic acid, chlorogenic acid, L-tyrosine and pyrogallol Trapa acornis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 70 PPO is stable at 20°C and 30°C for 20 min, and then the enzyme activity gradually decreases as time goes on. A decreased activity of 14.6% and 30% is observed after 50 min, respectively. The enzyme activity rapidly reduces at 40°C and 50°C as time goes on. After 50 min, the rudimental activities are only 43.7 and 10.6% of its original activity. The enzyme activity is nearly exhausted at 60°C and 70°C after 5 min Trapa acornis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
for L-tyrosine Trapa acornis
6
-
for catechol and caffeic acid Trapa acornis
7
-
for gallic acid, chlorogenic acid and pyrogallol Trapa acornis
8
-
for L-tyrosine Trapa acornis

pH Range

pH Minimum pH Maximum Comment Organism
3 9 enzyme activity decreases below pH 5.0 or above pH 8.0, however, the enzyme is still active at pH 3.0 and pH 9.0. PPO remains 77.96, 60.05 and 52.24% of its original activity between pH 5.0 and pH 7.0 using catechol, L-tyrosine and pyrogallol as substrates, respectively, and loses more than 57% of activity when using caffeic acid, gallic acid and chlorogenic acid as substrates at their optimum pH values Trapa acornis