Biochemical Analysis of Recombinant Pea Seed Coat-Specific Polyphenol Oxidase (PeaPPO) in Relation to Various Phenolic Substrates
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15640%2F25%3A73634527" target="_blank" >RIV/61989592:15640/25:73634527 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15310/25:73634527 RIV/00027006:_____/25:10179196
Result on the web
<a href="https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.5c01839" target="_blank" >https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.5c01839</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jafc.5c01839" target="_blank" >10.1021/acs.jafc.5c01839</a>
Alternative languages
Result language
angličtina
Original language name
Biochemical Analysis of Recombinant Pea Seed Coat-Specific Polyphenol Oxidase (PeaPPO) in Relation to Various Phenolic Substrates
Original language description
The seed coat serves as the primary protective barrier, offering mechanical and chemical defense for the embryo. It contains various metabolites, including phenolic compounds, which can be oxidized by polyphenol oxidase (PPO) to form oligomers. In this study, we heterologously expressed a 515 amino acid protein derived from wild pea (Pisum elatius), omitting its Nterminal signal sequence, and analyzed its biochemical properties. The recombinant PeaPPO required sodium dodecyl sulfate (SDS) for activation and exhibited activity between pHs 5.2 and 7.0, peaking at pH 6.0 with 0.25 mM SDS. Tropolone and its isomer thujaplicin were the most effective inhibitors. PeaPPO catalyzed reactions with seed coat-derived substrates, displaying activity toward phenols, catechols, and pyrogallols, with the highest affinity for catechols. Principal component analysis of LC-MS/MSderived phenolic profiles demonstrated that PPO+ and ppo− genotypes differ significantly in their accumulation of PPO substrates and inhibitors. These findings confirm that PeaPPO possesses both monophenolase and catechol oxidase activities, identifying it as a tyrosinase.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10611 - Plant sciences, botany
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
ISSN
0021-8561
e-ISSN
1520-5118
Volume of the periodical
73
Issue of the periodical within the volume
35
Country of publishing house
US - UNITED STATES
Number of pages
15
Pages from-to
21754-21768
UT code for WoS article
001554775100001
EID of the result in the Scopus database
2-s2.0-105015387526