Peach fruit ripening : a proteomic comparative analysis of the mesocarp of two cultivars with different flesh firmness at two ripening stages
Articolo
Data di Pubblicazione:
2011
Citazione:
Peach fruit ripening : a proteomic comparative analysis of the mesocarp of two cultivars with different flesh firmness at two ripening stages / B. Prinsi, A.S. Negri, C. Fedeli, S. Morgutti, N. Negrini, M. Cocucci, L. Espen. - In: PHYTOCHEMISTRY. - ISSN 0031-9422. - 72:10(2011 Jul), pp. 1251-1262. [10.1016/j.phytochem.2011.01.012]
Abstract:
A proteomic analysis was conducted on peach fruit mesocarp in order to better elucidate the biochemical
and physiological events which characterize the transition of fruit from the ‘‘unripe’’ to the ‘‘ripe’’ phase.
The first goal of the present work was to set-up a protocol suitable for improving protein extraction
from peach mesocarp. The use of freeze-dried powdered tissue, together with the addition of phenol prior
to the extraction with an aqueous buffer, significantly increased the protein yield and the quality of 2-DE
gels. The proteomic profiles of the mesocarp from peach fruit of a non-melting flesh (NMF; ‘Oro A’) and a
melting flesh (MF; ‘Bolero’) cultivar, at ‘‘unripe’’ and ‘‘ripe’’ stages as defined by some parameters typical
of ripening, were then analyzed.
The comparative analysis of the 2-DE gels showed that in NMF and MF peaches the relative volumes of
53 protein spots significantly changed in relation to both the ripening stage (‘‘unripe’’ versus ‘‘ripe’’) and/
or the genetic background of the cultivar (‘Oro A’ versus ‘Bolero’).
Thirty out of the 53 differently abundant spots were identified by LC–ESI-MS/MS. The analysis revealed
enzymes involved in primary metabolism (e.g. C-compounds, carbohydrates, organic acids and amino
acids) and in ethylene biosynthesis as well as proteins involved in secondary metabolism and responses
to stress.
Among these, 1-aminocyclopropane-1-carboxylic acid oxidase (ACO) appeared to be one of the proteins
with the largest change in relative abundance during the fruit transition from the pre-climacteric
(‘‘unripe’’) to the climacteric (‘‘ripe’’) phase. Other proteins, such as S-adenosylmethionine synthetase
and b-cyanoalanine synthase involved in ethylene metabolism, were also identified. Moreover, the
changes in the relative abundances of a sucrose synthase and an a-amylase suggested differences between
the two cultivars in the carbohydrate import activity of ripe fruit. The different accumulation of a few typical
ROS-scavenger enzymes suggested that a higher oxidative stress occurred in MF with respect to NMF
fruit. This result, together with data concerning the levels of total proteins and free amino acids and those
regarding proteins involved in the maintenance of tissue integrity, was consistent with the hypothesis that
the last phase of ripening in MF fruit is characterized by the appearance of a senescence status.
The present study appears to define well some of the biochemical and physiological events that characterize
the ripening of peach and, at the same time, provides interesting indications that could be employed
in future marker assisted selection (MAS) programmes aimed to obtain MF fruits with higher ability to
preserve tissue functionality maintaining for a longer time their organoleptic characteristics.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
(Non)melting flesh; climacteric; peach; protein extraction protocol; proteomic analysis; Prunus persica; ripening; rosaceae; senescence
Elenco autori:
B. Prinsi, A.S. Negri, C. Fedeli, S. Morgutti, N. Negrini, M. Cocucci, L. Espen
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