Characteristics of honey bee physiological proteins extracted from faba bean (Vicia faba L.) honey

Abstract

Faba bean (Vicia faba L.) is a valuable agricultural crop, widely used in the food industry and environmental protection. In this study, faba bean honey samples were subjected to quantitative and qualitative proteomic analysis. Using a direct mass spectrometry assay, a total of 45 honey bee (Apis mellifera) proteins were identified in faba bean honey, of which 18 were of known honey bee origin, and the others were uncharacterized honey bee proteins. Royal jelly proteins accounted for 39.29% of all known honey bee proteins identified in this study, while major royal jelly protein (MRJP-1) accounted for 47.06% of the royal jelly proteins. Honey bee proteins were separated from acid to basic isoelectric point (pI). Carboxyl ester hydrolase OS=Apis mellifera OX7460 was mostly an acidic protein and separated at pI 4.40. Transferrin OS=Apis mellifera was separated close to the neutral isoelectric point, at pI 6.73. Histone H2B OS=Apis mellifera OX7460 was mostly basic and its pI value was 10.82. The honey bee proteins identified in the faba bean honey confirm its naturalness and valuable enzymatic properties.