Nisin: A Novel Substrate for Glutathione S-Transferase Isolated from Fresh Beef
2002
Rose, N.L. | Palcic, M.M. | Sporns, P. | McMullen, L.M.
Little success has been reported on the use of the antimicrobial peptide nisin in meat products. Previous research in our laboratory hypothesized that nisin is inactivated in raw meat systems by an enzymatic reaction with glutathione. We isolated glutathione S-transferase from fresh beef muscle and examined the in vitro enzymatic reaction between nisin and glutathione. The products of the reaction were analyzed by antibacterial-activity assays and MALDI-TOF MS. Under optimum reaction temperatures, the results showed that 3 glutathione molecules could conjugate to 1 nisin molecule, suggesting that multiple dehydro residues are involved. Assays for antibacterial activity confirmed that all activity was lost. Results support the inactivation of nisin by glutathione.
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