Metastable radicals and intrinsic chemiluminescence from soy proteins

Chemiluminescence from various powdered food proteins were examined without the addition of any external source of free radicals or luminescent agents. In the solid-state, soy and whey proteins produced more intrinsic chemiluminescence than casein, sodium caseinate, or egg albumin. However, when these same food proteins were hydrated, intrinsic chemiluminescence from soy proteins was about 4- to 8-times greater than other source proteins. Quenching the alkyl-radicals in the powdered soy proteins with hydrogen sulfide reduced the typical electron paramagnetic resonance spectra from soy proteins below detectable levels, and reduced the chemiluminescence from the hydrated soy proteins by about 65%. Antioxidants also reduced chemiluminescence in hydrated soy proteins by about 50% to 92%, with ellagic acid being the most effective. The reduction in chemiluminescence from both quenching radicals in the solid state, and by the addition of antioxidants to aqueous mixtures, indicate that the chemiluminescence produced when soy proteins are hydrated is a free radical catalyzed event. Based on the production of chemiluminescence, the radicals from soy protein were largely released within 30 min of hydration at 23 °C. Elevating the hydration temperatures increased chemiluminescence by as much as 280% at 70 °C, and decreased the half-life of the light-emitting reaction by about 9-fold.

Levels of metastable radicals in powdered soy proteins typically range from to 10 to 100 times greater than free radicals from other food protein sources. This research focuses on the types of reactions these radicals catalyze when soy proteins are hydrated, and the radicals suddenly become reactive. The findings suggest that a portion of the energy released from metastable radicals when powdered soy proteins are hydrated is involved in the generation of chemically-induced light.