Foaming and emulsifying properties of fractions of gluten peptides obtained by limited enzymatic hydrolysis and ultrafiltration

Gluten hydrolysates were prepared by limited enzymatic hydrolysis with a protease having a chymotryptic activity in the presence or in the absence of cysteine during the dispersion phase of the process. The hydrolysates were fractionated by ultrafiltration, using two inorganic membranes with different molecular weight cut-off (MWCO), 50 kg/mol and 150 kg/mol. The retentates were enriched in hydrophobic peptides and the permeates were enriched in hydrophilic peptides. The foaming and emulsifying properties of hydrolysates, retentates and permeates were analysed at two pHs (4 and 6.5) and two salt concentrations (0.2 and 2% NaCl). Hydrolysates displayed a foaming capacity, but the foams were not stable. Permeates generated foams at pH 6.5 only, and these foams had a very short life-time. Permeates displayed no emulsifying properties. Retentates yielded foams with a good stability and were more efficient than whole hydrolysates to stabilise emulsions. They provided a strong resistance to coalescence. The functional properties of retentates were only sightly influenced by pH and ionic strength. Neither cysteine addition, which helps gluten dispersion and increases the yield of soluble hydrolysate, nor the MWCO of the ultrafiltration membranes influenced the functionality of the hydrolysate fractions. (C) 2002 Elsevier Science Ltd.