Gelation behaviors of denaturated pea albumin and globulin fractions during transglutaminase treatment

Abstract The behavior of pea albumins (Alb) and globulins (Glob) in a denatured state toward microbial transglutaminase (MTGase) treatment was studied by SDS-PAGE analysis, free amine group determination, dynamic rheology and confocal laser scanning microscopy. The denaturation of pea proteins by chemical reduction with dithiothreitol (DTT) or by thermal treatment at 80 °C enhanced the enzymatic crosslinking degree of both protein isolates with greater crosslinking for the Glob fraction. The chemical denaturation affected preferentially the participation in crosslinking reaction of legumin acid subunits (40 kDa) for Glob sample and albumin polypeptides PA2 (26 kDa) for Alb sample, whereas the heat treatment led to complete polymerization of 55, 35 and 30 kDa vicilin polypeptides for pea globulins as shown by SDS-PAGE analysis. Up to 10 wt% concentration, the Alb fraction was not able to form MTGase crosslinked gels whatever the initial native or denaturated state. Compared to the native state, chemical and thermal denaturation of Glob fraction before enzymatic treatment led to the formation of weaker and stronger viscoelastic gels respectively. These contradictory results indicated that the enzymatic crosslinking reaction is highly related to polypeptides composition and conformation of proteins and the use of denaturation as a strategy to enhance gel forming properties by transglutaminase treatment has to be used with caution in the case of plant proteins.