Proteolytic activity of selected commercial Lactobacillus helveticus strains on soy protein isolates.

Soy protein isolates were fermented by three commercial Lactobacillus helveticus strains for a maximum of seven days to investigate the resulting proteolysis. The proteolytic activity of the most active strain (LH88) was further analyzed (LC-MS/MS and GC-MS) and it was shown that the β-conglycinin α subunit 1, β-conglycinin α' subunit, glycinin G1, and 2S albumin were specifically degraded. Peptigram analysis and visualization of the crystal structure showed that the hydrolysis sites of β-conglycinin α subunit, α' subunit, and the glycinin G1 were located on the surface of the molecule or at the mobile disordered region, hence being highly accessible for the proteinase of LH88.

Casein-Based Powders: Characteristics and Rehydration Properties.

Casein-based powders are gaining industrial interest due to their nutritional and functional properties, but they are also known to have poor rehydration abilities. The fundamental physical and chemical mechanisms involved in the rehydration of these powders are essential for determining the critical steps in the manufacturing processes and for developing casein powders with improved rehydration properties. A number of analytical methods have been developed to measure the rehydration ability of powders, but criteria for the selection of methods for casein-based powders have not been provided.