Influence of Actinidin-Induced Hydrolysis on the Functional Properties of Milk Protein and Whey Protein Concentrates.

Abstract

The main aim of the study was to establish the impact of limited proteolysis by actinidin on the functionality of selected milk protein systems. The plant protease actinidin was used to produce hydrolysates (MPHs) from milk protein concentrate (MPC) and whey protein concentrate (WPC) to 0, 5, 10 or 15% of the degree of hydrolysis (DH) at an enzyme-to-substrate ratio of 1:100 (5.21 units of actinidin activity g-1 of protein). The functionalities assessed included solubility, heat stability, emulsification and foaming properties. In general, significant changes in the functionalities of MPH were associated with the extent of hydrolysis. Solubility of hydrolysates increased with increasing %DH, with WPC showing about 97% solubility at 15% DH. Emulsifying properties were negatively affected by hydrolysis, whereas heat stability was improved in the case of WPC (~25% of heat stability increased with an increase in DH to 15%). Hydrolysates from both WPC and MPC had improved foaming properties in comparison to unhydrolysed controls. These results were also supported by changes in the FTIR spectra. Further adjustment of hydrolysis parameters, processing conditions and pH control could be a promising approach to manipulate selected functionalities of MPHs obtained using actinidin.