It has been reported that Coffea arabica seeds contain as the main reserve protein, a legumin-like protein, constituted of two subunits, alpha and beta, of approximately 35 and 20 kDa. In this work the seed proteins of several coffee species and varieties were investigated by SDS-PAGE and gel filtration. No differences were observed in the electrophoretic profiles among varieties of C. arabica, however, marked differences were observed among species, or even among individuals of some species. In general, the molecular weight of the subunits alpha and beta accounted for a monomer of 48 to 62 kDa. However, native molecular weight obtained by gel filtration showed that for most of the species there is association of 6 of such proteins, in a hexamer. The most marked difference was observed for C. canephora and C. racemosa. The former clearly showing isoforms of the subunits, and the later showing absence of the beta subunit. The influence of proteases in this observations is discussed.
Coffea; legumin; endosperm
