Abstract
The functional properties of milk protein concentrate (MPC) powders are often hindered by their poor solubility. Calcium chelating salts have been shown to improve powder solubility, but generally their action contributes to higher viscosity due to disintegration of casein micelles and higher levels of serum-phase calcium. To help mitigate increases in viscosity associated with calcium chelation, transglutaminase (TGase), an enzyme that covalently crosslinks protein, was employed in an effort to stabilise the casein micelle structure. Sodium hexametaphosphate (SHMP) was added to control (C-MPC) and TGase crosslinked MPC (TG-MPC) dispersions at concentrations of 5, 12.5 and 25 mm prior to analysis. TG-MPC dispersions had lower viscosity than C-MPC dispersions across all SHMP concentrations studied. Crosslinking limited micelle dissociation on SHMP addition and led to greater retention of the white colour of the protein dispersions, while the turbidity of C-MPC dispersions decreased with increasing SHMP addition.
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