Thermodynamic activities of polar sites of collagen in the presence of CO2 were observed by inverse gas chromatographic techniques using water as a probe. The interactions between collagen and the water probe were evaluated by determining the specific retention volume (Vg°) and partition coefficient (Kp) at 25°C, 3°C, and 35°C. Thermodynamic parameters were determined from these data. CO2 exhibited a significant effect on the water binding of collagen as shown by increased Vg° and Kp values as compared to N2‐ and He‐treated collagen. The thermodynamic parameters of partial molar Gibb's free energy (ΔT°), partial molar enthalpy (ΔT°) and partial molar entropy (ΔT°) indicated CO2 significantly increased the average energy of water binding by collagen.
|Number of pages||4|
|Journal||Journal of Food Science|
|State||Published - Jul 1988|