RIMSI - Repository of Institute for Multidisciplinary Research
University of Belgrade - Institute for Multidisciplinary Research
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrillic)
    • Serbian (Latin)
  • Login
View Item 
  •   RIMSI
  • Institut za multidisciplinarna istraživanja
  • Radovi istraživača / Researchers’ publications
  • View Item
  •   RIMSI
  • Institut za multidisciplinarna istraživanja
  • Radovi istraživača / Researchers’ publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Characterisation of phenol oxidase and peroxidase from maize silk

No Thumbnail
Authors
Hadzi-Tasković Sukalović, Vesna
Veljović-Jovanović, Sonja
Dragišić Maksimović, Jelena
Maksimović, Vuk
Pajic, Zorica
Article (Published version)
Metadata
Show full item record
Abstract
Silk of some maize genotypes contains a high level of phenolics that undergo enzymatic oxidation to form quinones, which condense among themselves or with proteins to form brown pigments. Two phenolic oxidizing enzymes, peroxidase (POD; EC 1.11.1.7) and polyphenol oxidase (PPO; EC 1.10.3.1), from maize (Zea mays L.) silk were characterised with respect to their preferred substrate, different isoforms and specific effectors. One browning silk sample with high, and two non-browning samples with low phenolic content were investigated. Although POD oxidizes a wide range of phenolic substrates in vitro, its activity rate was independent of silk phenolic content. PPO activity, detected with o-diphenolic substrates, was abundant only in browning silk, and low or absent in non-browning silk. Pollination increased POD but not PPO activity. Isoelectric-focusing (IEF) and specific staining for POD and PPO showed a high degree of polymorphism that varied with silk origin. The IEF pattern of POD re...vealed a number of anionic and several cationic isoenzymes, with the most pronounced having neutral pI 7 and a basic isoform with pI 10. Detected isoforms of PPO were anionic, except for one neutral form found only in browning silk, and occupied positions different from those of POD. Different inhibitory effects of NaN3, EDTA, KCN, and L-cysteine, as well as different impacts of a variety of cations on the oxidation of chlorogenic acid, mediated by PPO or POD, were detected. The findings are discussed in terms of a possible roles of these enzymes in defence and pollination.

Keywords:
polyphenol oxidase / Phenolic compounds / peroxidase
Source:
Plant Biology, 2010, 12, 3, 406-413
Publisher:
  • Wiley-Blackwell, Hoboken
Funding / projects:
  • Oplemenjivanje kukuruza specifičnih svojstava za industrijske potrebe (RS-20003)
  • Regulacija antioksidativnog metabolizma biljaka u toku rastenja, infekcije patogenima i delovanja abiotičkog stresa: mehanizmi transporta, signalizacije i otpornosti (RS-143020)

DOI: 10.1111/j.1438-8677.2009.00237.x

ISSN: 1435-8603

PubMed: 20522176

WoS: 000276618400003

Scopus: 2-s2.0-84971280048
[ Google Scholar ]
13
9
URI
http://rimsi.imsi.bg.ac.rs/handle/123456789/399
Collections
  • Radovi istraživača / Researchers’ publications
Institution/Community
Institut za multidisciplinarna istraživanja
TY  - JOUR
AU  - Hadzi-Tasković Sukalović, Vesna
AU  - Veljović-Jovanović, Sonja
AU  - Dragišić Maksimović, Jelena
AU  - Maksimović, Vuk
AU  - Pajic, Zorica
PY  - 2010
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/399
AB  - Silk of some maize genotypes contains a high level of phenolics that undergo enzymatic oxidation to form quinones, which condense among themselves or with proteins to form brown pigments. Two phenolic oxidizing enzymes, peroxidase (POD; EC 1.11.1.7) and polyphenol oxidase (PPO; EC 1.10.3.1), from maize (Zea mays L.) silk were characterised with respect to their preferred substrate, different isoforms and specific effectors. One browning silk sample with high, and two non-browning samples with low phenolic content were investigated. Although POD oxidizes a wide range of phenolic substrates in vitro, its activity rate was independent of silk phenolic content. PPO activity, detected with o-diphenolic substrates, was abundant only in browning silk, and low or absent in non-browning silk. Pollination increased POD but not PPO activity. Isoelectric-focusing (IEF) and specific staining for POD and PPO showed a high degree of polymorphism that varied with silk origin. The IEF pattern of POD revealed a number of anionic and several cationic isoenzymes, with the most pronounced having neutral pI 7 and a basic isoform with pI 10. Detected isoforms of PPO were anionic, except for one neutral form found only in browning silk, and occupied positions different from those of POD. Different inhibitory effects of NaN3, EDTA, KCN, and L-cysteine, as well as different impacts of a variety of cations on the oxidation of chlorogenic acid, mediated by PPO or POD, were detected. The findings are discussed in terms of a possible roles of these enzymes in defence and pollination.
PB  - Wiley-Blackwell, Hoboken
T2  - Plant Biology
T1  - Characterisation of phenol oxidase and peroxidase from maize silk
EP  - 413
IS  - 3
SP  - 406
VL  - 12
DO  - 10.1111/j.1438-8677.2009.00237.x
ER  - 
@article{
author = "Hadzi-Tasković Sukalović, Vesna and Veljović-Jovanović, Sonja and Dragišić Maksimović, Jelena and Maksimović, Vuk and Pajic, Zorica",
year = "2010",
abstract = "Silk of some maize genotypes contains a high level of phenolics that undergo enzymatic oxidation to form quinones, which condense among themselves or with proteins to form brown pigments. Two phenolic oxidizing enzymes, peroxidase (POD; EC 1.11.1.7) and polyphenol oxidase (PPO; EC 1.10.3.1), from maize (Zea mays L.) silk were characterised with respect to their preferred substrate, different isoforms and specific effectors. One browning silk sample with high, and two non-browning samples with low phenolic content were investigated. Although POD oxidizes a wide range of phenolic substrates in vitro, its activity rate was independent of silk phenolic content. PPO activity, detected with o-diphenolic substrates, was abundant only in browning silk, and low or absent in non-browning silk. Pollination increased POD but not PPO activity. Isoelectric-focusing (IEF) and specific staining for POD and PPO showed a high degree of polymorphism that varied with silk origin. The IEF pattern of POD revealed a number of anionic and several cationic isoenzymes, with the most pronounced having neutral pI 7 and a basic isoform with pI 10. Detected isoforms of PPO were anionic, except for one neutral form found only in browning silk, and occupied positions different from those of POD. Different inhibitory effects of NaN3, EDTA, KCN, and L-cysteine, as well as different impacts of a variety of cations on the oxidation of chlorogenic acid, mediated by PPO or POD, were detected. The findings are discussed in terms of a possible roles of these enzymes in defence and pollination.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Plant Biology",
title = "Characterisation of phenol oxidase and peroxidase from maize silk",
pages = "413-406",
number = "3",
volume = "12",
doi = "10.1111/j.1438-8677.2009.00237.x"
}
Hadzi-Tasković Sukalović, V., Veljović-Jovanović, S., Dragišić Maksimović, J., Maksimović, V.,& Pajic, Z.. (2010). Characterisation of phenol oxidase and peroxidase from maize silk. in Plant Biology
Wiley-Blackwell, Hoboken., 12(3), 406-413.
https://doi.org/10.1111/j.1438-8677.2009.00237.x
Hadzi-Tasković Sukalović V, Veljović-Jovanović S, Dragišić Maksimović J, Maksimović V, Pajic Z. Characterisation of phenol oxidase and peroxidase from maize silk. in Plant Biology. 2010;12(3):406-413.
doi:10.1111/j.1438-8677.2009.00237.x .
Hadzi-Tasković Sukalović, Vesna, Veljović-Jovanović, Sonja, Dragišić Maksimović, Jelena, Maksimović, Vuk, Pajic, Zorica, "Characterisation of phenol oxidase and peroxidase from maize silk" in Plant Biology, 12, no. 3 (2010):406-413,
https://doi.org/10.1111/j.1438-8677.2009.00237.x . .

DSpace software copyright © 2002-2015  DuraSpace
About RIMSI | Send Feedback

OpenAIRERCUB
 

 

All of DSpaceCommunitiesAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About RIMSI | Send Feedback

OpenAIRERCUB