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Proteome changes of fresh-cut Zizania latifolia during refrigerated (1 °C) storage
The total proteins from the fresh-cut Zizania latifolia during refrigerated storage were extracted and separated by two-dimensional electrophoresis (2-DE). A total of 657 protein spots were detected on the gels, among which 33 spots showed a significant change in protein abundance based on twofold d...
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Published in: | European food research & technology 2012-12, Vol.235 (6), p.1011-1021 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The total proteins from the fresh-cut
Zizania latifolia
during refrigerated storage were extracted and separated by two-dimensional electrophoresis (2-DE). A total of 657 protein spots were detected on the gels, among which 33 spots showed a significant change in protein abundance based on twofold difference. Using MALDI-TOF/TOF, 25 spots were identified, which were classified into five functional categories that included cell structure (32 %), stress response and defense (28 %), ripening and senescence (8 %), signal transduction (8 %), and unclear functional proteins (24 %). Of the 25 differentially expressed proteins, 10 were up-regulated and 15 were down-regulated. Among 10 up-regulated spots, 5 were related to cell structure, 2 to oxidative stress, 1 to ripening and senescence, 1 to signal transduction, and 1 to unclear functional proteins. For the 15 down-regulated spots, 5 were related to stress response, 3 to cell structure, 1 to ripening and senescence, 1 to signal transduction, and 5 to unclear functional proteins. These results indicate that specific proteins expressed in fresh-cut
Z. latifolia
during storage at 1 °C show a coordinated response to cope with wounding stress caused by fresh-cut processing. |
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ISSN: | 1438-2377 1438-2385 |
DOI: | 10.1007/s00217-012-1828-2 |