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
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.
Mots clés
BSA, Carboxymethyllysine, Glycation, Glyoxal
Référence
Food Chem. 2023 07 4;428:136815