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Title: Papaya fruit softening: Role of hydrolases
Authors: Siwaporn Thumdee
Ashariya Manenoi
Nancy J. Chen
Robert E. Paull
Keywords: Agricultural and Biological Sciences
Biochemistry, Genetics and Molecular Biology
Issue Date: 29-Mar-2010
Abstract: Papaya (Carica papaya L.) cultivars show a wide variation in fruit softening rates, a character that determines fruit quality and shelf life, and thought to be the result of cell wall degradation. The activity of pectin methylesterase, β-galactosidase, endoglucanase, endoxylanase and xylosidase were correlated with normal softening, though no relationship was found between polygalacturonase activity and softening. When softening was modified by 1-MCP treatment, a delay occurred before the normal increase in activities of all cell wall activities except endoxylanase which was completely suppressed. Significant cell wall mass loss occurred in the mesocarp tissue during normal softening, but did not occur to the same extent following 1-MCP treatment. During normal softening, pectin polysaccharides and loosely bound matrix polysaccharides were solubilized and the release of xylosyl and galactosyl residues occurred. Cell wall changes in galactosyl residues after 1-MCP treatment were comparable to those of untreated fruit but 1-MCP treated fruit did not soften completely. The changes in the cell wall fractions containing xylosyl residues in 1-MCP treated fruit showed less solubilization and a higher association of xylosyl residues with the pectic polysaccharides. The results indicated that normal modification of cell wall xylosyl components during ripening did not occur following 1-MCP treatment at the color-break stage, this was associated with the failure of these fruit to fully soften and a selective suppression of endoxylanase activity. The results support a role for endoxylanase in normal papaya fruit softening and its suppression by 1-MCP lead to a failure to fully soften. Normal papaya ripening related softening was dependent upon the expression and activity of endoglucanase, β-galactosidase and endoxylanase. © 2010 Springer Science+Business Media, LLC.
ISSN: 19359764
Appears in Collections:CMUL: Journal Articles

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