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Article Dans Une Revue Colloids and Surfaces A: Physicochemical and Engineering Aspects Année : 2015

Monitoring of transglutaminase crosslinking reaction by 1H NMR spectroscopy on model substrates

Résumé

A new method based on 1H NMR spectroscopy was developed for monitoring transglutaminase crosslinking reaction with model molecules (CBZ-Gln-Gly and N-α-acetyl-lysine). The transglutaminase reaction led to the appearance of new resonances on NMR spectrum as well as significant decrease in others. The new observed resonances, originated from newly formed ɛ-(γ-glutamyl)lysine isopeptide bonds, evidence the enzymatic reaction and allow to quantify the ɛ-(γ-glutamyl)lysine fragment. Moreover, the decrease in resonance intensity, originated from lysine, permit to determine the crosslinking degree. These results obtained by 1H NMR spectroscopy can be used as an alternative method to LC–MS, reducing drastically the analysis time from 7 days to 2 h.
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Dates et versions

hal-02413068 , version 1 (16-12-2019)

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Attaf Djoullah, Nicolas Sok, Yanis Djemaoune, Marie-José Penouilh, Florence Husson, et al.. Monitoring of transglutaminase crosslinking reaction by 1H NMR spectroscopy on model substrates. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2015, 475, pp.69-74. ⟨10.1016/j.colsurfa.2014.12.066⟩. ⟨hal-02413068⟩
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