Abstract
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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The authors acknowledge the financial support from Foundation of Zhejiang Educational Committee (Y201226170) and together with the project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD).
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Luo, H., Bao, Y., Jiang, J. et al. Proteome changes of fresh-cut Zizania latifolia during refrigerated (1 °C) storage. Eur Food Res Technol 235, 1011–1021 (2012). https://doi.org/10.1007/s00217-012-1828-2
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DOI: https://doi.org/10.1007/s00217-012-1828-2