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1H NMR Spectroscopy As Tool To Study Transglutaminase Crosslinking Of Pea Globulin
Abstract : A new method based on NMR spectroscopy was developed to detect the G-L (GlutamylLysine) isopeptide bonds formed by the enzymatic transglutaminase reaction. Because of the
complexity of NMR signals of proteins due to their structures, the method was first developed
on a model system (glutamine and lysine) to simplify the detection of the G-L residue. And
then, the results were applied on the real protein matrix (pea globulin). MTG treatment of
model system led to the appearance of a new resonance on NMR spectrum which is
originated probably from the ε-methylene protons of lysine residues covalently linked to
glutamine. The comparison between NMR spectra of MTG-treated and untreated pea globulin
with MTG-treated model system permitted to identify the G-L isopeptide signal. The G-L
isopeptide signal is also observed in the NMR spectra of native pea globulin (untreated which
MTG), indicating that the isopeptide is naturally present in pea proteins. However, the
superimposition of NMR spectra of MTG-treated and untreated pea globulin shows a higher
intensity of G-L isopeptide signal for MTG-treated samples. The increased signal intensity
evidences the enzymatic reaction and permits to quantify the G-L isopeptide.
https://hal-agrosup-dijon.archives-ouvertes.fr/hal-02413499
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Submitted on : Monday, December 16, 2019 - 11:23:47 AM
Last modification on : Tuesday, December 8, 2020 - 10:00:05 AM
Contributor : Admin Agrosupdijon Connect in order to contact the contributor
Submitted on : Monday, December 16, 2019 - 11:23:47 AM
Last modification on : Tuesday, December 8, 2020 - 10:00:05 AM
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