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ACE-Inhibitory Activity of Whey Proteins Fractions Derived of Fermentation by Lacticaseibacillus rhamnosus GG and Streptococcus thermophilus SY-102.

Laura Berenice Olvera-RosalesEmmanuel Pérez-EscalanteAraceli Castañeda-OvandoElizabeth Contreras-LópezAlma-Elizabeth Cruz-GuerreroPatricia RegalAlejandra Cardelle-CobasLuis-Guillermo González-Olivares
Published in: Foods (Basel, Switzerland) (2023)
Many studies have reported the benefits of probiotic microorganisms and the production of angiotensin-converting enzyme (ACE) inhibitors. Determining the proteolytic and ACE inhibition capacities during whey fermentation was the goal of the study. Lacticaseibacillus rhamnosus GG, Streptococcus thermophilus SY-102, and both bacteria together were initially inoculated into whey, reaching an initial concentration of 10 8 CFU per milliliter in each fermentation system. Through the use of TNBS, SDS-PAGE, and SEC-HPLC methods, the proteolytic profile was examined. An in vitro investigation was performed to test the ACE inhibition capacity. With S. thermophilus , the logarithmic phase of microbial development was shorter than with L. rhamnosus (6 and 12 h, respectively). The logarithmic phase in the co-culture fermentation, however, was extended to 24 h. There were no significant differences in pH between the fermentations. However, the co-culture had a greater concentration of protein hydrolysis (453 ± 0.06 μg/mL), as indicated by the amount of free amino groups. Similarly, this fermentation produced more low molecular weight peptides. The higher inhibition activity, which increased at the conclusion of the fermentation with the co-culture and reached 53.42%, was influenced by the higher peptide synthesis. These findings highlighted the significance of creating useful co-culture products.
Keyphrases
  • angiotensin converting enzyme
  • saccharomyces cerevisiae
  • lactic acid
  • angiotensin ii
  • candida albicans
  • biofilm formation
  • mass spectrometry
  • small molecule
  • high resolution
  • tandem mass spectrometry