Assessment of the floral origin of honey via proteomic tools

Francesco Di Girolamo, Alfonsina D'Amato, Pier Giorgio Righetti

Research output: Contribution to journalArticlepeer-review


The honey from chestnut, acacia, sunflower, eucalyptus and orange was analysed for its proteome content, in order to see if any plant proteins present would allow the proteo-typing of these different varieties. Since the total protein content turned out to be minute, 200. g of each honey type were diluted to 1. L and then added with ProteoMiner to enhance the visibility of the proteinaceous material. All bands visible in the SDS-PAGE profile of each type of honey were eluted, digested and identified by mass spectrometry in a LTQ-XL instrument. It turned out that all proteins identified (except one, the enzyme glyceraldehyde-3-phosphate dehydrogenase from Mesembryanthemum crystallinum) were not of plant origin but belonged to the Apis mellifera proteome. Among the total proteins identified (eight, but only seven as basic constituents of all types of honey) five belonged to the family of major royal jelly proteins 1-5, and were also the most abundant ones in any type of honey, together with α-glucosidase and defensin-1. It thus appears that honey has a proteome resembling the royal jelly proteome (but with considerably fewer species), except that its protein concentration is lower by three to four orders of magnitude as compared to royal jelly. Attempts at identifying additional plant (pollen, nectar) proteins via peptidome analysis were unsuccessful.

Original languageEnglish
Pages (from-to)3688-3693
Number of pages6
JournalJournal of Proteomics
Issue number12
Publication statusPublished - Jun 27 2012


  • Hexapeptide ligands
  • Honey proteome
  • Low-abundance proteome
  • Peptide libraries
  • ProteoMiner
  • Royal jelly

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics


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