Probiotic properties and proteomics analysis of ethanol-induced Lactococcus lactis subsp. lactis IL1403

Chen, Sisi; Yi, Juanjuan; Suo, Keke; Kang, Qiaozhen; Lu, Laizheng; Lu, Jike

doi:10.1007/s11274-023-03627-y

Cited by 4 publications

(2 citation statements)

References 40 publications

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“…To identify these proteins, differential expression profiles of L. lactis were compared under ethanol stress, resulting in the identification of 216 upregulated proteins (fold change >1.5 and P < 0.05) . To select potential BAPs, the study collected amino acid sequence information from 216 stress-related proteins of L.…”

Section: Methodsmentioning

confidence: 99%

“…Our previous research observed that intracellular extracts of Lactococcus lactis (L. lactis) induced by ethanol increased ADH activity and improved alcohol metabolism in mice, suggesting that BAPs presented in stress-related proteins might play a relevant role. , In another study, proteins related to stress and metabolism, which were abundantly synthesized during yeast propagation, were identified as significant precursors of BAPs . It was hypothesized that the ethanol stress-related proteins of L.…”

Section: Introductionmentioning

confidence: 99%

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Identification of a Novel Peptide with Alcohol Dehydrogenase Activating Ability from Ethanol-Induced Lactococcus lactis: A Combined In Silico Prediction and In Vivo Validation

Chen,

Yi,

Kang

et al. 2024

J. Agric. Food Chem.

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Alcohol dehydrogenase (ADH) is a crucial rate-limiting enzyme in alcohol metabolism. Our previous research found that ethanol-induced intracellular extracts of Lactococcus lactis (L. lactis) could enhance alcohol metabolism in mice, but the responsible compounds remain unidentified. The study aimed to screen potential ADH-activating peptides from ethanol-induced L. lactis using virtual screening and molecular docking calculation. Among them, the pentapeptide FAPEG might bind to ADH through hydrophobic interaction and hydrogen bonds, then enhancing ADH activity. Spectroscopy analysis further investigated the peptide-enzyme interaction between FAPEG and ADH, including changes in the amino acid residue microenvironment and secondary structural alterations. Furthermore, FAPEG could protect against alcoholic liver injury (ALI) in mice by reducing blood alcohol concentration, enhancing the activity of antioxidant and alcohol metabolism enzymes, and attenuating alcohol-induced hepatotoxicity, which was related to the activation of the Nrf2/keap1/HO-1 signaling pathway. The study provided preliminary evidence that the generation of ADH-activating peptides in ethanol-induced L. lactis has the potential in preventing ALI in mice using in silico prediction and in vivo validation approaches.

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Section: Methodsmentioning

confidence: 99%