Antioxidative food pigments during manufacturing are subjected to harsh conditions that can attenuate the antioxidant benefits and alter its color significantly. Thus, stabilization of these pigments is desired to increase the product's nutritional and commercial value. Ribulose-1, 5-bisphosphate carboxylase oxygenase (RuBisCO), an abundant protein with a balanced amino acid profile, may serve as a good binding agent to increase stability of pigments due to the fact that it is naturally bound to chlorophyll in plants besides its highly stable structure. This research investigated the binding capacity of purified RuBisCO to riboflavin, annatto extract, and beta-carotene. Protein-pigment complexes were promoted with mixing, sonicating, heating and freeze thawing techniques. Raman spectroscopy, surface plasmon resonance, and UV-Vis were used to measure binding potential. A method to extract RuBisCO from tobacco with paramagnetic antibody-coated beads was also investigated. Not only does this exploratory research provide the baseline understanding of the challenges and hurdles in forming a protein-pigment complex, but the detection techniques established could also be of value for developing quantitative measurements of such complexes. While further research is still needed to elucidate the interaction between the pigments and RuBisCO, it was confirmed that the binding ability of RuBisCo to the pigments investigated could be greatly hindered by the structural conformation of RuBisCo.