Sodium Chloride Suppresses the Bitterness of Protein Hydrolysates by Decreasing Hydrophobic Interactions.

Abstract

The formation of bitter off-flavor is a long-existing issue during food protein hydrolysis. The aim of this study is to determine the mechanism of sodium chloride (NaCl) suppressing the bitterness of protein hydrolysates. In this study, the bitterness of egg white hydrolysate (EWH) and hen meat hydrolysate (HPH) was determined using an electronic tongue. The results showed that the bitterness intensity of quinine hydrochloride, EWH, and HPH was suppressed significantly by NaCl in a concentration-dependent manner (P<0.05). The particle sizes, turbidity, zeta potentials, and surface hydrophobicity of EWH and HPH were also significantly decreased by NaCl at concentrations of 0.05, 0.1, 0.3, and 0.5M (P<0.05). These results indicated that adding NaCl at certain concentrations led to a salting-in effect, burying hydrophobic groups and decreasing the surface hydrophobicity of peptides, resulting in the decrease of bitterness. Using NaCl is an alternative, effective, and cheap strategy to suppress protein hydrolysate bitterness by decreasing hydrophobic interactions in food industry. PRACTICAL APPLICATION: NaCl can be used as an effective bitterness masker for food protein hydrolysates by decreasing hydrophobic interactions of peptides.