Abstract:
: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.
journal_name
Food Chemjournal_title
Food chemistryauthors
Shirotani N,Bygvraa Hougaard A,Lametsch R,Agerlin Petersen M,Rattray FP,Ipsen Rdoi
10.1016/j.foodchem.2020.128152subject
Has Abstractpub_date
2021-03-15 00:00:00pages
128152eissn
0308-8146issn
1873-7072pii
S0308-8146(20)32014-8journal_volume
340pub_type
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