Thermal gelation in relation to binding of bovine serum albumin polysaccharide systems

Thermal gelation of bovine serum albumin (BSA)-sodium alginate, BSA-pectin and BSA-methyl cellulose systems in relation to binding was studied using rheological testing, turbidimetric analysis and gel filtration. Two electrostatic binding mechanisms, distinguished by particle and chain segment binding models were found in BSA-anionic polysaccharide systems. Particle binding resulted in poor gelation properties. Positive effects on gelation were found when conditions favored the chain segment binding model. Mechanisms for gelation-binding relationships were hypothesized. No evidence of binding was found in the BSA-methyl cellulose system, which generally exhibited the combined gelation properties of the individual components.