Effects of enzyme activities during steeping and sprouting on the solubility and composition of proteins, their bioactivity and relationship with the bread making quality of wheat flour

The aim was to determine the effect of steeping and sprouting on wheat grain proteins and the functional consequences in this regard. The solubility of proteins and the polypeptide composition of albumins, globulins, gliadins and glutenins were determined, as well as the content of non-protein nitrogen and free sulfhydryl groups (-SH), and the activity of peroxidase (POD) and lipoxygenase (LOX). In addition, the pasting viscosity of flour and protein bioactivity such as antioxidant capacity and immunoreactivity were evaluated. The increase of non-protein nitrogen and free -SH groups by about 62.09 and 96.7%, respectively, as well as the decrease of albumin + globulin polypeptides with a molecular weight over 85.94 kDa and between 85.94-48.00 kDa by about 34 and 8.7%, respectively, were the most notable changes observed in the flour from whole sprouted wheat that clearly point to the intensive protein hydrolysis. The reduction of disulfide bonds and increased concentrations of free -SH groups significantly modify the visco-elastic properties of gliadins and glutenins causing pasting viscosity reduction. However, sprouted wheat flour could be considered as a potential food ingredient because of its improved antioxidant capacity that is a result of protein hydrolysis inter alia. As protein modification induced by steeping may have beneficial effects on the antigenicity of the glutenin fraction, this kind of wheat pretreatment can represent a putative strategy in the dietary modulation of diseases related to glutenin immunoreactivity, e.g. dermatitis herpetiformis