Abstract:
Flavor is a major determinant of consumer acceptance of a food product. Flavor compounds added to food products can interact with protein presented in food and may result in the reduction of flavor intensity (flavor fade). The objective of this study was to study the effect of enzymatic deamidation by protein-glutaminase (PG) on the flavor-binding property of coconut protein by equilibrium dialysis technique using vanillin as a model. Three percent (w/v) of untreated coconut protein (CP) and deamidated coconut protein (DCP) in 0.05 M phosphate buffer (pH = 7.0) were bound to vanillin at different concentrations (10 - 100 ppm) and temperatures (5, 15, and 25 °C). Binding parameters, including number of binding site (n) and binding constant (K), were derived from Klotz plots. The results show that deamidation by PG (36.12 % degree of deamidation) could decrease overall flavor-binding affinity (nK) of the protein to vanillin. In addition, the nK was decreased with increasing in temperature. The thermodynamic parameters of binding indicated that the vanillin-protein interactions were spontaneous (- ∆G°). Furthermore, the interactions were driven by enthalpy. Mechanism of the binding of CP and DCP to vanillin were suggested as van der Waals forces or hydrogen bonding. It was also found that odor detection threshold of vanillin in DCP sample was lower than in CP. From the results indicated that the deamidation of coconut protein by PG can decrease the binding of coconut protein to vanillin. It was also found that small molecular proteins were increased after deamidation.