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

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 Chem

journal_title

Food chemistry

authors

Shirotani N,Bygvraa Hougaard A,Lametsch R,Agerlin Petersen M,Rattray FP,Ipsen R

doi

10.1016/j.foodchem.2020.128152

subject

Has Abstract

pub_date

2021-03-15 00:00:00

pages

128152

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(20)32014-8

journal_volume

340

pub_type

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