Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction
Reaction mixtures containing peanut protein isolate (PPI) and dextran (1: 1 weight ratio)
were dry-heated at 60° C and 79% relative humidity for 7days. SDS–PAGE analysis
indicated that PPI had become complexed with dextran to form conjugates of higher
molecular weight. Arachin, accounting for 50% of peanut proteins, was hard to glycosylate
with dextran, which might limit the extent of glycosylation of PPI. The thermal stability of PPI
was remarkably improved by mixture/conjugation with dextran. Proteins in …
were dry-heated at 60° C and 79% relative humidity for 7days. SDS–PAGE analysis
indicated that PPI had become complexed with dextran to form conjugates of higher
molecular weight. Arachin, accounting for 50% of peanut proteins, was hard to glycosylate
with dextran, which might limit the extent of glycosylation of PPI. The thermal stability of PPI
was remarkably improved by mixture/conjugation with dextran. Proteins in …
Reaction mixtures containing peanut protein isolate (PPI) and dextran (1:1 weight ratio) were dry-heated at 60°C and 79% relative humidity for 7days. SDS–PAGE analysis indicated that PPI had become complexed with dextran to form conjugates of higher molecular weight. Arachin, accounting for 50% of peanut proteins, was hard to glycosylate with dextran, which might limit the extent of glycosylation of PPI. The thermal stability of PPI was remarkably improved by mixture/conjugation with dextran. Proteins in mixtures/conjugates might have a more compacted tertiary conformation than PPI. The protein solubility of conjugates at pH 4.5–6.0 was remarkably increased compared with the PPI/mixture. Mixture with dextran could significantly improve the emulsifying and foaming properties of PPI (p<0.05). Conjugation with dextran could further enhance emulsifying and foaming properties of PPI.
Elsevier
