Transglutaminase-catalyzed Amination of Pea Protein Peptides Using the Biogenic Amines Histamine and Tyramine

Background: Biogenic amines (BAs) are produced by the enzymatic decarboxylation of amino acids, and are well-known for their toxicity to humans. This study describes a new method using microbial transglutaminase (MTGase) to covalently link BAs such as histamine (HIS) and tyramine (TYR) to the glutamine residues of alcalase-hydrolyzed pea protein (PPH).

Results: The incubation of PPH and HIS and TYR in the presence of MTGase at 37 °C led to the formation of conjugates, as determined by liquid chromatography, after derivatization with dansyl chloride. Seventy-six % of HIS and 65% of TYR were covalently incorporated to PPH by MTGase. The incubation of PPH and TYR in the presence of MTGase exhibited a 52% DPPH radical scavenging activity at 10 mg mL . Conjugation via MTGase improved the antioxidant status by reducing lipid peroxidation.

Conclusion: This study emphasizes that the application of MTGase can effectively reduce histamine and tyramine content while simultaneously enhancing antioxidative capacity of PPH. © 2016 Society of Chemical Industry.