Tri-ethylene glycol (TEG) is an effective plasticizer for many protein-based thermoplastics because of its low volatility, however, partial miscibility with the protein matrix may still lead to some phase separation. Spatial variation of TEG concentration in bloodmeal-based thermoplastics as a result of processing was investigated using synchrotron-based FT-IR micro-spectroscopy. Although TEG forms strong hydrogen bonding with proteins, for the protein to fold into β-sheets bound plasticizer must be released. TEG can then migrate, pooling into localized areas, rich in plasticizer. Further heating causes further migration towards the edge of plasticized bloodmeal particles where the TEG may evaporate. Thermo-gravimetric analysis confirmed th...