| Title |
Antioxidant protein signatures in honey: botanical influence and proteomic variability |
| Authors |
Čeksterytė, Violeta ; Kaupinis, Algirdas ; Gvazdauskė, Gabrielė ; Navakauskienė, Rūta ; Jaškūnė, Kristina |
| DOI |
10.1016/j.fochx.2026.103647 |
| Full Text |
|
| Is Part of |
Food chemistry: X.. Elsevier Ltd.. 2026, vol. 34, art. no. 103647, p. [1-9].. eISSN 2590-1575 |
| Keywords [eng] |
antioxidant proteins ; authenticity ; honey proteomics ; LC–MS ; oilseed rape, botanical origin ; pollen |
| Abstract [eng] |
Antioxidant capacity of honey derives from both polypHenols and proteins. We aimed to define putative antioxidant-protein signatures across honeys of differing botanical origin and relate them to pollen for authenticity assessment. Seven Lithuanian honeys were profiled by LC-MS proteomics, identifying 17 proteins with annotated antioxidant function (10 plant-, 6 bee-, 1 aphid-derived). Plant proteins, dominated by Brassica napus, were most abundant in monofloral B. napus honey. Bee proteins, glucose-methanol-choline oxidoreductases, were more variable and together comprised >75% of the summed antioxidant-protein signal. Correlations showed positive associations between B. napus pollen and most B. napus-derived proteins (r = 0.815–0.996) but not with bee-derived proteins; chalcone–flavonone isomerase correlated negatively. Fold-change analysis in comparison to monofloral B. napus honey confirmed up-regulation of B. napus proteins and down-regulation of several bee oxidoreductases. Altogether, plant proteins capture botanical origin, whereas bee proteins reflect apicultural factors, supporting a multi-indicator basis for honey authenticity and functional appraisal. |
| Published |
Elsevier Ltd |
| Type |
Journal article |
| Language |
English |
| Publication date |
2026 |
| CC license |
|
