• Lb. helveticus LH88 partly degrades soy protein to free amino acids and volatiles. • High specificity for β-conglycinin (α and α' subunit), glycinin G1 and 2S albumin. • Hydrolysis sites were located on the surface or the mobile disordered region. 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. The proteins were partially further degraded to free amino acids, and subsequently catabolized to volatile compounds. However, most of the proteins remained native, even after seven days of fermentation, thus additional modification of protein structure or adjustment of fermentation conditions are required for effective generation of flavor compounds. [ABSTRACT FROM AUTHOR]