Glycated bovine serum albumin for use in feeding trials with animal models - In vitro methodology and characterization of a glycated substrate for modifying feed pellets.

Fiche publication

Date publication

juillet 2023

Journal

Food chemistry

Auteurs

Membres identifiés du Cancéropôle Est :
Pr GILLERY Philippe

Tous les auteurs :
Nogueira Silva Lima MT, Howsam M, Delayre-Orthez C, Jacolot P, Jaisson S, Criquet J, Billamboz M, Ghinet A, Fradin C, Boulanger E, Bray F, Flament S, Rolando C, Gillery P, Niquet-Léridon C, Tessier FJ

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/37450953

Résumé

This study investigated different methods to produce N-carboxymethyl-lysine (CML)-enriched bovine serum albumin (BSA) as alternatives to the classical approach using glyoxylic acid (GA) and sodium cyanoborohydride (NaBHCN) which results in toxic hydrogen cyanide (HCN). The reaction of GA (6 mmol/L) and NaBHCN (21 mmol/L) to produce CML remained the most effective with CML yields of 24-35%, followed by 13-24% using 300 mmol/L glyoxal (GO). GA promoted specific modification of lysine to CML, and fewer structural modifications of the BSA molecule compared with GO, as evidenced by fluorescence and proteomic analyses. GO promoted greater arginine modification compared with GA (76 vs 23%). Despite structural changes to BSA with GO, murine fecal clearance of CML was similar to literature values. Hence, BSA glycation with 300 mmol/L glyoxal is a suitable alternative to GA and NaBHCN for generating CML-enriched protein free of HCN, but a CML-only fortification model remains to be described.