Inhibitory activity of a Concanavalin-isolated fraction from a glucosamine-peptides reaction system against heat resistant E. coli

Alcalase-derived gelatin hydrolysates were glycated with glucosamine in the presence (+) or absence (−) of transglutaminase (TGase), and their antimicrobial activities toward Escherichia coli AW 1.7 were studied. Glycation treatments were subjected to concanavalin A affinity chromatography to selectively collect the glycopeptide-enriched fractions and the changes in antimicrobial activity were determined. The minimum inhibitory concentration of glycated hydrolysates decreased by 1.2 times compared to the native hydrolysate, with no differences between (+) or (−) TGase treatments. No difference was observed in the dicarbonyl compound concentration between the two glycation methods except that 3-deoxyglucosone was greater in the TGase-mediated reaction. Concanavalin A-retentate, but not the flow-through fractions, significantly improved the antimicrobial activity, however there was no difference between +TGase and −TGase glycated treatments. Purification of the retentate fraction from fluorescent compounds did not improve its antimicrobial activity.