Search results for "pea globulin"
showing 6 items of 6 documents
Native-state pea albumin and globulin behavior upon transglutaminase treatment
2015
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…
Effects of heat treatment on rheological properties of pea and egg white protein mixtures
2020
International audience; Partial substitution of animal protein by plant protein is a new opportunity to produce sustainable food for human beings. However, separated studies of plant protein and egg white cannot help to have a direct understanding of the complex structure in a mixed food product. In this work, we used low-denatured pea globulins (PG) in admixture with raw egg white (EW) to study the thermal and rheological behavior of the mixed systems submitted to heat treatment (>G’’) for all the protein samples whatever the pH. Higher storage modulus (G’) values for egg white indicated stronger elastic behavior as for the mixtures. From strain sweep experiments, the addition of PG in the…
1H NMR Spectroscopy As Tool To Study Transglutaminase Crosslinking Of Pea Globulin
2013
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…
Enzymatic cross-linking of pea proteins to produce microparticles : application to the encapsulation of riboflavin
2015
In this work, pea proteins behavior toward enzymatic gelation by microbial transglutaminase (MTGase) was studied at native state and after denaturation (chemical reduction or thermal denaturation). The final application was the formation of protein microparticules to encapsulate riboflavin, chosen as hydrophilic active molecule model. The extraction process of the pea protein fractions has been optimized in such a way to minimize as possible protein denaturation and recover native fractions rich in albumin (Alb) and globulin (Glob) or a mixture of both.The setting up of the enzymatic reaction monitoring methods has brought out their complementarity as well as their limits. Two new monitorin…
Rheological properties of thermal gels of pea and egg white protein mixtures
2021
International audience; Partial substitution of animal protein by plant protein is a new opportunity to produce sustainable food for human beings. However, separated studies of plant protein and egg white cannot help to have a direct understanding of the complex structure in a mixed food product. In this work, we used low-denatured pea globulins (PG) in admixture with raw egg white (EW) to study the thermal and rheological behavior of the mixed systems submitted to heat treatment (>G’’) for all the protein samples whatever the pH. Higher storage modulus (G’) values for egg white indicated stronger elastic behavior as for the mixtures. From strain sweep experiments, the addition of PG in the…
Etude des interactions dans la formation d'agrégats thermiques mixtes entre globulines de pois et béta-lactoglobuline : application à l'élaboration d…
2016
In the context of protein source diversification, pea protein is a promising ingredient and may be associated with milk proteins such as whey proteins in the production of new food products. In the present work, the thermal aggregation (85°C - 1 h) of pea globulins (Glob) alone and in admixture with β-lactoglobulin (βlg), prior to acid gelation, was studied as a function of total protein concentration, βlg/Glob weight ratio and ionic strength. The characterization of soluble aggregates was carried out by combining different analytical methods such as surface hydrophobicity determination, disulfide bridge quantification, dynamic light scattering (DLS), size exclusion chromatography (SEC-HPLC…