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Transglutaminase‐catalyzed amination of pea protein peptides using the biogenic amines histamine and tyramine
Author(s) -
Lu Xinyao,
Hrynets Yuliya,
Betti Mirko
Publication year - 2017
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.8057
Subject(s) - chemistry , dansyl chloride , tyramine , hydrolysis , decarboxylation , reductive amination , biochemistry , chromatography , covalent bond , amino acid , organic chemistry , derivatization , high performance liquid chromatography , catalysis
Abstract 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 −1 . 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