Isolated 7S and 11S globulins obtained from defeated soy flour were complexated with folic acid (FA) in order to generate nano-carriers for this important vitamin in human nutrition. Fluorescence spectroscopy and dynamic light scattering were applied to follow the nano-complexes formation and for their characterization. Fluorescence experimental data were modeled by the Stern-Volmer and a modified double logarithm approach. The results obtained confirmed static quenching. The number of binding sites on the protein molecule was ~1. The values obtained for the binding constants suggest a high affinity between proteins and FA. Particle size distribution allowed to study the protein aggregation phenomenon induced by FA bound to the native proteins. Z-average manifested a clear trend to protein aggregation. 11S-FA nano-complexes resulted in more polydispersity. ζ-potential of FA nano-complexes did not show a remarkable change after FA complexation. The biological activity of nano-complexes loaded with FA was explored in terms of their capacity to enhance the biomass formation of Lactobacillus casei BL23. The results concerning to nano-complexes inclusion in culture media showed higher bacterial growth. Such a result was attributed to the entry of the acid by the specific receptors concomitantly by the peptide receptors. These findings have technological impact for the use of globulins-FA based nano-complexes in nutraceutical, pharmaceutical and food industries.