Fermented Supernatants of Lactobacillus plantarum GKM3 and Bifidobacterium lactis GKK2 Protect against Protein Glycation and Inhibit Glycated Protein Ligation

Nutrients. 2023 Jan 5;15(2):277. doi: 10.3390/nu15020277.

Abstract

With age, protein glycation in organisms increases continuously. Evidence from many studies shows that the accumulation of glycated protein is highly correlated with biological aging and the development of aging-related diseases, so developing a dietary agent to attenuate protein glycation is very meaningful. Previous studies have indicated that lactic acid bacteria-fermented products have diverse biological activities especially in anti-aging, so this study was aimed to investigate the inhibitory effect of the fermented supernatants of Lactobacillus plantarum GKM3 (GKM3) and Bifidobacterium lactis GKK2 (GKK2) on protein glycation. The results show that GKM3- and GKK2-fermented supernatants can significantly inhibit protein glycation by capturing a glycation agent (methylglyoxal) and/or protecting functional groups in protein against methylglyoxal-induced responses. GKM3- and GKK2-fermented supernatants can also significantly inhibit the binding of glycated proteins to the receptor for advanced glycation end products (RAGE). In conclusion, lactic acid bacteria fermentation products have the potential to attenuate biological aging by inhibiting protein glycation.

Keywords: Bifidobacterium lactis GKK2; Lactobacillus plantarum GKM3; aging; fermented supernatants; protein glycation; the receptor for advanced glycation end products (RAGE).

MeSH terms

  • Bifidobacterium animalis*
  • Fermentation
  • Glycated Proteins
  • Lactobacillus plantarum* / metabolism
  • Maillard Reaction
  • Pyruvaldehyde / metabolism

Substances

  • Glycated Proteins
  • Pyruvaldehyde

Grants and funding

This research received no external funding.