Selective proteolysis of ?-conglycinin as a tool to increase air-water interface and foam stabilising properties of soy proteins

Proteolysis of food proteins changes their conformation and often generates bioactive peptides, leading to improved nutritional value techno-functional properties. Protein isolates that originated from plants are generally a mixture several proteins. Enzymatic hydrolysis such mixtures has drawback, as it is unclear which in the hydrolysed, poorly reproducible outcomes. In present study, we applied controlled methodology, called selective proteolysis, investigated its effects on air-water interface foam stabilising properties soy protein isolate (SPI). We selectively hydrolysed 7S ?-conglycinin SPI, while 11S glycinin remained relatively intact. Hydrolysates were obtained at two different degrees (DH). Selective resulted increased surface activity, higher foamability, nearly doubled. The size peptides seemed significantly affect mechanical layer interface, was studied by removing smaller than 14 kDa via dialysis. Peptides found hinder interfacial network formation, larger stiffness. This also reflected stability, hydrolysate with low DH stability hydrolysates DH. demonstrated proteolysis can increase properties, could lead new healthy more sustainable products.