Fermentation of Gluten by Lactococcus lactis LLGKC18 Reduces its Antigenicity and Allergenicity

Probiotics Antimicrob Proteins. 2022 Oct;14(5):779-791. doi: 10.1007/s12602-021-09808-1. Epub 2021 Jun 3.

Abstract

Wheat is a worldwide staple food, yet some people suffer from strong immunological reactions after ingesting wheat-based products. Lactic acid bacteria (LAB) constitute a promising approach to reduce wheat allergenicity because of their proteolytic system. In this study, 172 LAB strains were screened for their proteolytic activity on gluten proteins and α-amylase inhibitors (ATIs) by SDS-PAGE and RP-HPLC. Gliadins, glutenins, and ATI antigenicity and allergenicity were assessed by Western blot/Dot blot and by degranulation assay using RBL-SX38 cells. The screening resulted in selecting 9 high gluten proteolytic strains belonging to two species: Enterococcus faecalis and Lactococcus lactis. Proteomic analysis showed that one of selected strains, Lc. lactis LLGKC18, caused degradation of the main gluten allergenic proteins. A significant decrease of the gliadins, glutenins, and ATI antigenicity was observed after fermentation of gluten by Lc. lactis LLGKC18, regardless the antibody used in the tests. Also, the allergenicity as measured by the RBL-SX38 cell degranulation test was significantly reduced. These results indicate that Lc. lactis LLGKC18 gluten fermentation can be deeply explored for its capability to hydrolyze the epitopes responsible for wheat allergy.

Keywords: Epitopes; Gliadins; LAB fermentation; Lactococcus lactis; Peptidomic; RBLSX38 degranulation; Specific IgE; Wheat allergy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / metabolism
  • Fermentation
  • Gliadin / metabolism
  • Glutens / metabolism
  • Humans
  • Immunoglobulin E / metabolism
  • Lactobacillales* / metabolism
  • Lactococcus lactis* / metabolism
  • Proteomics

Substances

  • Allergens
  • Immunoglobulin E
  • Glutens
  • Gliadin