Publications

2025

• ACL - Articles comité de lecture référencés bases de données AERES

  Study on rapeseed albumin hydrolysis by PrtS protease from Streptococcus thermophilus and bioactivity characterization of resulting hydrolysates

  Foods, 14 (13), pp. 2235-2235.

  Hafeez, Z., Beaubier, S., Aymes, A., Christophe, S., Akbar, S., Kapel, R., Miclo, L.

  See the abstract Consulter le lien

  Lactic acid bacteria are well known for hydrolyzing milk proteins, but their application to
  plant proteins remains limited. This study evaluated the ability of the cell-wall-anchored
  PrtS protease from two Streptococcus thermophilus strains to hydrolyze rapeseed albumins
  (RAs), aiming to generate bioactive peptides with potential food functionality. The specific
  activity of PrtS was first determined using a chromogenic substrate. RAs were then
  hydrolyzed using 10X- and 100X-concentrated cell pellets of each strain to assess the hydrolysis
  kinetics and the enzymatic mechanism. The results showed concentration-dependent
  hydrolysis, with protein conversion and the degree of hydrolysis increasing threefold at
  100X for both strains. Despite the increased hydrolysis, the peptides produced had similar
  average sizes, averaging at five amino acids, indicating a consistent “one-by-one” cleavage
  mechanism. The in vitro testing of the RA hydrolysates produced with 100X PrtS from
  S. thermophilus LMD-9 revealed dose-dependent antioxidant activity comparable to native
  RAs. Importantly, unlike native RAs, these hydrolysates did not induce increased secretion
  of the pro-inflammatory mediator IL-8 in inflamed HT-29 cells, suggesting a reduced proinflammatory
  potential. These findings demonstrate that PrtS protease from S. thermophilus
  can effectively hydrolyze rapeseed proteins to produce functional hydrolysates with improved
  bioactivity profiles. Such hydrolysates have promising applications as functional
  ingredients in plant-based food products, contributing both to health benefits and potential
  food preservation through antioxidant activity.

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