Proteome changes of fresh-cut Zizania latifolia during refrigerated (1 °C) storage

• DOI: 10.1007/s00217-012-1828-2
• Publication Date: 2012-12-22T11:32:40Z
• Authors: Haibo Luo; Yonghua Bao; Juan Jiang; Li Zhang; Liuli Song; Li Jiang; Zhifang Yu
• Keywords: Proteome

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.