Pectin methylesterases induce an abrupt increase of acidic pectin during strawberry fruit ripening

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Abstract

The decrease of strawberry (Fragariaxananassa Duch.) fruit firmness observed during ripening is partly attributed to pectolytic enzymes: polygalacturonases, pectate lyases and pectin methylesterases (PMEs). In this study, PME activity and pectin content and esterification degree were measured in cell walls from ripening fruits. Small green, large green, white, turning, red and over-ripe fruits from the Elsanta cultivar were analyzed. Using the 2F4 antibody directed against the calcium-induced egg box conformation of pectin, we show that calcium-bound acidic pectin was nearly absent from green and white fruits, but increased abruptly at the turning stage, while the total pectin content decreased only slightly as maturation proceeded. Isoelectrofocalisation performed on wall protein extracts revealed the expression of at least six different basic PME isoforms. Maximum PME activity was detected in green fruits and steadily decreased to reach a minimum in senescent fruits. The preliminary role of PMEs and subsequent pectin degradation by pectolytic enzymes is discussed.
Original languageEnglish
Pages (from-to)1152-60
Number of pages9
JournalJournal of plant physiology
Volume165
Issue number11
DOIs
Publication statusPublished - 31 Jul 2008

Fingerprint

Fragaria
pectinesterase
pectins
strawberries
Fruit
ripening
fruits
pectate lyase
Calcium
Polygalacturonase
calcium
Esterification
esterification
Enzymes
polygalacturonase
enzymes
Cell Wall
Ovum
firmness
pectin

Keywords

  • Pectins
  • Carboxylic Ester Hydrolases
  • Esterification
  • Acids
  • Isoenzymes
  • Fruit
  • Fragaria
  • Isoelectric Focusing

Cite this

@article{885bcb96b73c44c6b406cc04e14ac697,
title = "Pectin methylesterases induce an abrupt increase of acidic pectin during strawberry fruit ripening",
abstract = "The decrease of strawberry (Fragariaxananassa Duch.) fruit firmness observed during ripening is partly attributed to pectolytic enzymes: polygalacturonases, pectate lyases and pectin methylesterases (PMEs). In this study, PME activity and pectin content and esterification degree were measured in cell walls from ripening fruits. Small green, large green, white, turning, red and over-ripe fruits from the Elsanta cultivar were analyzed. Using the 2F4 antibody directed against the calcium-induced egg box conformation of pectin, we show that calcium-bound acidic pectin was nearly absent from green and white fruits, but increased abruptly at the turning stage, while the total pectin content decreased only slightly as maturation proceeded. Isoelectrofocalisation performed on wall protein extracts revealed the expression of at least six different basic PME isoforms. Maximum PME activity was detected in green fruits and steadily decreased to reach a minimum in senescent fruits. The preliminary role of PMEs and subsequent pectin degradation by pectolytic enzymes is discussed.",
keywords = "Pectins, Carboxylic Ester Hydrolases, Esterification, Acids, Isoenzymes, Fruit, Fragaria, Isoelectric Focusing",
author = "Mallory Draye and {Van Cutsem}, Pierre",
year = "2008",
month = "7",
day = "31",
doi = "10.1016/j.jplph.2007.10.006",
language = "English",
volume = "165",
pages = "1152--60",
journal = "Journal of plant physiology",
issn = "0176-1617",
publisher = "Urban und Fischer Verlag GmbH und Co. KG",
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TY - JOUR

T1 - Pectin methylesterases induce an abrupt increase of acidic pectin during strawberry fruit ripening

AU - Draye, Mallory

AU - Van Cutsem, Pierre

PY - 2008/7/31

Y1 - 2008/7/31

N2 - The decrease of strawberry (Fragariaxananassa Duch.) fruit firmness observed during ripening is partly attributed to pectolytic enzymes: polygalacturonases, pectate lyases and pectin methylesterases (PMEs). In this study, PME activity and pectin content and esterification degree were measured in cell walls from ripening fruits. Small green, large green, white, turning, red and over-ripe fruits from the Elsanta cultivar were analyzed. Using the 2F4 antibody directed against the calcium-induced egg box conformation of pectin, we show that calcium-bound acidic pectin was nearly absent from green and white fruits, but increased abruptly at the turning stage, while the total pectin content decreased only slightly as maturation proceeded. Isoelectrofocalisation performed on wall protein extracts revealed the expression of at least six different basic PME isoforms. Maximum PME activity was detected in green fruits and steadily decreased to reach a minimum in senescent fruits. The preliminary role of PMEs and subsequent pectin degradation by pectolytic enzymes is discussed.

AB - The decrease of strawberry (Fragariaxananassa Duch.) fruit firmness observed during ripening is partly attributed to pectolytic enzymes: polygalacturonases, pectate lyases and pectin methylesterases (PMEs). In this study, PME activity and pectin content and esterification degree were measured in cell walls from ripening fruits. Small green, large green, white, turning, red and over-ripe fruits from the Elsanta cultivar were analyzed. Using the 2F4 antibody directed against the calcium-induced egg box conformation of pectin, we show that calcium-bound acidic pectin was nearly absent from green and white fruits, but increased abruptly at the turning stage, while the total pectin content decreased only slightly as maturation proceeded. Isoelectrofocalisation performed on wall protein extracts revealed the expression of at least six different basic PME isoforms. Maximum PME activity was detected in green fruits and steadily decreased to reach a minimum in senescent fruits. The preliminary role of PMEs and subsequent pectin degradation by pectolytic enzymes is discussed.

KW - Pectins

KW - Carboxylic Ester Hydrolases

KW - Esterification

KW - Acids

KW - Isoenzymes

KW - Fruit

KW - Fragaria

KW - Isoelectric Focusing

U2 - 10.1016/j.jplph.2007.10.006

DO - 10.1016/j.jplph.2007.10.006

M3 - Article

C2 - 18160124

VL - 165

SP - 1152

EP - 1160

JO - Journal of plant physiology

JF - Journal of plant physiology

SN - 0176-1617

IS - 11

ER -