Apidologie 32 (2001) 69-80
Some properties of the main protein of honeybee (Apis mellifera) royal jellyJozef Simúth
Laboratory for Genetic Engineering, Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, 84238 Bratislava, Slovak Republic
(Received 7 July 2000; revised 16 October 2000; accepted 25 October 2000)
Royal jelly (RJ) was separated by ultracentrifugation (245000 g for 5 h at 6 oC) into three physically distinct fractions with different distribution of its components (proteins, sugars and fatty acids): yellowish fluid supernatant (61% w/w of RJ), yellowish-brown gelatinous sediment (32% w/w) and white nearly solid sediment (7% , w/w). Ultracentrifugation of the solvated gelatinous fraction was a suitable method for preparation of MRJP1, the most abundant protein of RJ in the form of gel. MRJP1 was present in RJ in different forms: a monomer (55 kDa), oligomeric subunit (ca. 420 kDa), and water-insoluble aggregates in sediment after its interaction with fatty acids. The oligomeric MRJP1 was well soluble in water and at concentrations of 30 to 50% (w/w) formed a stiff gel. It is suggested that MRJP1 is albumin-like protein. An interesting feature of the oligomeric form of MRJP1 is its ability for self-assembly in water solutions.
Key words: honeybee royal jelly / ultracentrifugation / oligomeric albumin-like protein / gel formation / self-assembly
Correspondence and reprints: Jozef Simúth
© INRA, EDP Sciences, DIB, AGIB 2001