Soybeans' value may be improved by modifying their storage protein content to broaden soy food product markets. To find novel storage proteins, hence bringing new texture to soyfood, would expand the variety of soy products available on the market. Storage proteins from the globulin family such as glycinin (11S) and beta-conglycinin (7S) play an essential role in soyfood production. The objectives of this study were: 1) to assess the potential of using the genetic diversity found in G. soja to modify G. max storage protein profile; 2) to identify novel proteins formed by the combination of protein subunits coming from an interspecific cross and; 3) to validate protein QTLs found in a F2 population in an F5. The genetic material used in this study was a F5 RIL population derived from the cross G. soja (PI458536) x G. max (NK S08-80). The 2D-gel analyses revealed a difference in several seed storage protein subunits between S08-80 and PI458536, both compositionally and quantitatively. The main difference was for the acidic glycinin level, which was more intense in NK S08-80 than in PI458536, making the 11S/7S ratio higher in PI458536. No differences were found for the beta-conglycinin level.