Transglutaminase‐catalyzed amination of pea protein peptides using the biogenic amines histamine and tyramine. (26th October 2016)

• Record Type: Journal Article
• Authors: Lu, Xinyao; Hrynets, Yuliya; Betti, Mirko
• Is Part Of: Journal of the science of food and agriculture. Volume 97:Number 8(2017)
• Page Start: 2436
• Page End: 2442
• Publication Date: 2016-10-26
• Subjects: biogenic amines -- transglutaminase -- pea protein hydrolysate -- conjugation -- antioxidant capacity; Food -- Periodicals; Agriculture -- Periodicals; 664
• DOI: 10.1002/jsfa.8057
• Languages: English
• ISSNs: 0022-5142

Abstract

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