0000000000329183
AUTHOR
Yanis Djemaoune
Native-state pea albumin and globulin behavior upon transglutaminase treatment
International audience; The behavior of pea albumin (Alb) and globulin (Glob) in their native state upon microbial transglutaminase (MTGase) treatment was studied. Only Glob was able to form a gel, at up to a 10% (w/w) concentration, with a minimum gelling concentration of 6% (w/w), and with a cross-linking degree of 25%. The most affected Glob subunits were convicilin (71 kDa), vicilins (55, 50, and 35 kDa), and legumin acidic subunit (40 kDa). In contrast, the legumin basic subunit (20 kDa) and vicilins of molecular weight less than 20 kDa remained mostly intact in all studied conditions. The cross-linking degree of Alb was 12%, which was not sufficient to form MTGase-induced gel. Major a…
1H NMR Spectroscopy As Tool To Study Transglutaminase Crosslinking Of Pea Globulin
Skiathos Island, GREECE - 30 May - 02 June 2013; International audience; 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 thecomplexity of NMR signals of proteins due to their structures, the method was first developedon a model system (glutamine and lysine) to simplify the detection of the G-L residue. Andthen, the results were applied on the real protein matrix (pea globulin). MTG treatment ofmodel system led to the appearance of a new resonance on NMR spectrum which isoriginated probably from the ε-methylene protons of lysine residues covalently linked toglutamine. The co…
Monitoring of transglutaminase crosslinking reaction by 1H NMR spectroscopy on model substrates
International audience; 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 …