Izvorni znanstveni članak
https://doi.org/10.1515/aiht-2015-66-2653
Major royal jelly proteins as markers of authenticity and quality of honey
Katarina Bilikova
; Institute of Forest Ecology, SAS, Zvolen, Slovakia
Tatiana Kristof Krakova
; Institute of Forest Ecology, SAS, Zvolen, Slovakia
Kikuji Yamaguchi
; Japan Royal Jelly Co., Ltd., Tokyo, Japan
Yoshihisa Yamaguchi
; Japan Royal Jelly Co., Ltd., Tokyo, Japan
Sažetak
Until now, the properties of honey have been defined based exclusively on the content of plant components in the nectar of given plant. We showed that apalbumin1, the major royal jelly (RJ) protein, is an authentic and regular component of honey. Apalbumin1 and other RJ proteins and peptides are responsible for the immunostimulatory properties and antibiotic activity of honey. For the quantification of apalbumin1, an enzyme-linked immunosorbent assay (ELISA) was developed using polyclonal anti-apalbumin1 antibody. The method is suitable for honey authenticity determination; moreover it is useful for detection of the honey, honeybee pollen and RJ in products of medicine, pharmacy, cosmetics, and food industry, where presences of these honeybee products are declared. Results from the analysis for presence and amount of apalbumin1 in honeys will be used for high-throughput screening of honey samples over the world. On the basis of our experiments which show that royal jelly proteins are regular and physiologically active components of honey we propose to change the definition of honey (according to the EU Honey Directive 2001/110/EC) as follows: Honey is a natural sweet substance produced by honey bees from nectar of plants or from secretions of plants, or excretions of plant sucking insects, which honey bees collect, transform by combining with major royal jelly proteins and other specific substances of their own, deposit, dehydrate, store and leave in the honey comb to ripen and mature.
Ključne riječi
royal jelly proteins; antimicrobial peptides; honey authenticity
Hrčak ID:
149568
URI
Datum izdavanja:
16.12.2015.
Posjeta: 2.732 *