Paper · 2007 · International Journal of Chemical Reactor Engineering

Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase

Serap Dogan; Pinar Turan; Mehmet Dogan; et al.

13
claims
32
verbatim quotes
4
citations
1
research areas
—
Not open access

Abstract

The paper reports the inhibition model of the purified polyphenol oxidase (PPO) activity from basil (Ocimum basilicum L.) with L-cysteine, ethylenediaminetetraacetic acid (EDTA), ascorbic acid, gallic acid, D,L-dithiothreitol, tropolone, glutathione, sodium azide, benzoic acid, salicylic acid and 4-aminobenzoic acid inhibitors using 4-methylcatechol, catechol and pyrogallol as substrates. The inhibitors such as salicylic acid, benzoic acid and EDTA did not inhibit Ocimum basilicum L. PPO for all substrates used in this study. Purification was carried out by precipitation of contaminating proteins with (NH4)2O4 dialysis of the supernatant and a Sepharose 4B-L-tyrosine-p-aminobenzoic acid affinity chromatography. The enzyme-catalysed browning reaction was significantly inhibited in the presence of L-cysteine, ascorbic acid, gallic acid, D,L-dithiothreitol, tropolone, glutathione, sodium azide and 4-aminobenzoic acid inhibitors. It was found that the inhibition types were (i) competitive inhibition for L-cysteine, ascorbic acid, D,L-dithiothreitol, tropolone and sodium azide inhibitors using 4-methylcatechol as a substrate; for L-cysteine, ascorbic acid, gallic acid, tropolone and glutathione inhibitors using catechol as a substrate; and for ascorbic acid inhibitor using pyrogallol as a substrate, (ii) uncompetitive inhibition for gallic acid inhibitor using 4-methylcatechol as a substrate; for 4-aminobenzoic acid inhibitor using catechol as a substrate; for tropolone and 4-aminobenzoic acid inhibitors using pyrogallol as a substrate, (iii) noncompetitive inhibition for 4-aminobenzoic acid inhibitor using 4-methylcatechol as a substrate; for D,L-dithiothreitol and sodium azide inhibitors using catechol as a substrate; and for L-cysteine, glutathione and sodium azide inhibitors using pyrogallol as a substrate. Furthermore, tropolone was the most effective inhibitor for Ocimum basilicum L. PPO because of its low KI value. Results showed that the type of inhibition depended on the origin of the PPO studied and also on the substrate used.

Abstract from the paper’s OpenAlex record, shown for indexing and research. Copyright remains with the authors or the publisher. Read at the source ↗

The text the model read, with the source record’s inline markup (italics, sub- and superscripts) rendered and its character entities decoded; quote offsets refer to the raw text.

Claims 13

Intervention effectobservedoriginal resultno effectmeasured

Claim · model-written summary

Salicylic acid, benzoic acid and EDTA did not inhibit basil PPO for any substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
salicylic acid, benzoic acid and EDTAe1
Outcome
Ocimum basilicum L. PPOe1
Direction
did not inhibite1

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“The inhibitors such as salicylic acid, benzoic acid and EDTA did not inhibit Ocimum basilicum L. PPO for all substrates used in this study”

✓ located verbatim in the source · abstract, characters 392–530 · show in text ↑
Intervention effectobservedoriginal resultsignificant (as stated)measured

Claim · model-written summary

L-cysteine, ascorbic acid, gallic acid, D,L-dithiothreitol, tropolone, glutathione, sodium azide and 4-aminobenzoic acid significantly inhibited the enzyme-catalysed browning reaction of basil PPO.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
L-cysteine, ascorbic acid, gallic acid, D,L-dithiothreitol, tropolone, glutathione, sodium azide and 4-aminobenzoic acide2
Outcome
enzyme-catalysed browning reactione2
Direction
significantly inhibitede2

Not reportedComparator

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e2

“The enzyme-catalysed browning reaction was significantly inhibited in the presence of L-cysteine, ascorbic acid, gallic acid, D,L-dithiothreitol, tropolone, glutathione, sodium azide and 4-aminobenzoic acid inhibitors”

✓ located verbatim in the source · abstract, characters 721–938 · show in text ↑
Observationobservedoriginal resultpositivemeasured

Claim · model-written summary

Tropolone was the most effective inhibitor of basil PPO, because of its low KI value.

Taxon
Ocimum basilicumOcimum basilicumt0
Compound
tropolonee3
Outcome
most effective inhibitore3
Qualifier
because of its low KI valuee3

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e3

“tropolone was the most effective inhibitor for Ocimum basilicum L. PPO because of its low KI value”

✓ located verbatim in the source · abstract, characters 1851–1949 · show in text ↑
Associationobservedoriginal resultmeasured

Claim · model-written summary

The type of inhibition depended on the origin of the PPO and on the substrate used.

Taxon
Ocimum basilicumOcimum basilicumt0
Gene
PPOe4
Outcome
type of inhibitione4
Direction
depended one4

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e4

“Results showed that the type of inhibition depended on the origin of the PPO studied and also on the substrate used”

✓ located verbatim in the source · abstract, characters 1951–2066 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Competitive inhibition of basil PPO by L-cysteine, ascorbic acid, D,L-dithiothreitol, tropolone and sodium azide with 4-methylcatechol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
L-cysteine, ascorbic acid, D,L-dithiothreitol, tropolone and sodium azidee1
Outcome
competitive inhibitione1
Qualifier
using 4-methylcatechol as a substratee1

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“competitive inhibition for L-cysteine, ascorbic acid, D,L-dithiothreitol, tropolone and sodium azide inhibitors using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 988–1137 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Competitive inhibition of basil PPO by L-cysteine, ascorbic acid, gallic acid, tropolone and glutathione with catechol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
L-cysteine, ascorbic acid, gallic acid, tropolone and glutathionee2
Outcome
competitive inhibitione1
Qualifier
using catechol as a substratee2

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“competitive inhibition for L-cysteine, ascorbic acid, D,L-dithiothreitol, tropolone and sodium azide inhibitors using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 988–1137 · show in text ↑
e2

“for L-cysteine, ascorbic acid, gallic acid, tropolone and glutathione inhibitors using catechol as a substrate”

✓ located verbatim in the source · abstract, characters 1139–1249 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Competitive inhibition of basil PPO by ascorbic acid with pyrogallol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
ascorbic acide2
Outcome
competitive inhibitione1
Qualifier
using pyrogallol as a substratee2

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“competitive inhibition for L-cysteine, ascorbic acid, D,L-dithiothreitol, tropolone and sodium azide inhibitors using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 988–1137 · show in text ↑
e2

“for ascorbic acid inhibitor using pyrogallol as a substrate”

✓ located verbatim in the source · abstract, characters 1255–1314 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Uncompetitive inhibition of basil PPO by gallic acid with 4-methylcatechol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
gallic acide1
Outcome
uncompetitive inhibitione1
Qualifier
using 4-methylcatechol as a substratee1

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“uncompetitive inhibition for gallic acid inhibitor using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 1321–1409 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Uncompetitive inhibition of basil PPO by 4-aminobenzoic acid with catechol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
4-aminobenzoic acide2
Outcome
uncompetitive inhibitione1
Qualifier
using catechol as a substratee2

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“uncompetitive inhibition for gallic acid inhibitor using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 1321–1409 · show in text ↑
e2

“for 4-aminobenzoic acid inhibitor using catechol as a substrate”

✓ located verbatim in the source · abstract, characters 1411–1474 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Uncompetitive inhibition of basil PPO by tropolone and 4-aminobenzoic acid with pyrogallol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
tropolone and 4-aminobenzoic acide2
Outcome
uncompetitive inhibitione1
Qualifier
using pyrogallol as a substratee2

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“uncompetitive inhibition for gallic acid inhibitor using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 1321–1409 · show in text ↑
e2

“for tropolone and 4-aminobenzoic acid inhibitors using pyrogallol as a substrate”

✓ located verbatim in the source · abstract, characters 1476–1556 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Noncompetitive inhibition of basil PPO by 4-aminobenzoic acid with 4-methylcatechol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
4-aminobenzoic acide1
Outcome
noncompetitive inhibitione1
Qualifier
using 4-methylcatechol as a substratee1

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“noncompetitive inhibition for 4-aminobenzoic acid inhibitor using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 1564–1661 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Noncompetitive inhibition of basil PPO by D,L-dithiothreitol and sodium azide with catechol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
D,L-dithiothreitol and sodium azidee2
Outcome
noncompetitive inhibitione1
Qualifier
using catechol as a substratee2

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“noncompetitive inhibition for 4-aminobenzoic acid inhibitor using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 1564–1661 · show in text ↑
e2

“for D,L-dithiothreitol and sodium azide inhibitors using catechol as a substrate”

✓ located verbatim in the source · abstract, characters 1663–1743 · show in text ↑
Intervention effectobservedoriginal resultmeasured

Claim · model-written summary

Noncompetitive inhibition of basil PPO by L-cysteine, glutathione and sodium azide with pyrogallol as substrate.

Taxon
Ocimum basilicumOcimum basilicumt0
Treatment
L-cysteine, glutathione and sodium azidee2
Outcome
noncompetitive inhibitione1
Qualifier
using pyrogallol as a substratee2

Not reportedComparatorDirection

Organisms pictured · Representative pictures of the matched species, not figures from the paper.

Ocimum basilicum
Ocimum basilicum · TaxonCastielli · CC BY-SA 3.0 · Wikimedia Commons ↗

Verbatim

t0

“Inhibition Kinetic of Ocimum basilicum L. Polyphenol Oxidase”

✓ located verbatim in the source · title, characters 0–60 · show in text ↑
e1

“noncompetitive inhibition for 4-aminobenzoic acid inhibitor using 4-methylcatechol as a substrate”

✓ located verbatim in the source · abstract, characters 1564–1661 · show in text ↑
e2

“for L-cysteine, glutathione and sodium azide inhibitors using pyrogallol as a substrate”

✓ located verbatim in the source · abstract, characters 1749–1836 · show in text ↑

salicylic acid · physiology: antioxidant enzymes · Ocimum basilicum (basil)Positive and negative results

4 papers: 3 positive, 1 negative or no effect

3 in the opposite direction

  1. positive
  2. positive
  3. positive
See all 4 papers →

Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.