Effect of Protein-Glutaminase on Calcium Sulphate-Induced Gels of SPI with Different Thermal Treatments

Abstract

The effects of protein-glutaminase (PG) on calcium sulphate (CaSO4)-induced gels of soy protein isolate (SPI) with different heat treatment levels were investigated. The time-dependent degree of deamidation showed that the mild denaturation of the protein favored the deamidation. The particle size distribution showed that the heat treatment increased the SPI particle size, and the particle size distribution of the SPI shifted to the right or increased the proportion of the large particle size component as the degree of deamidation increased for each sample. Rheological analysis showed that the deamidation substantially pushed up the gel temperature and decreased the value of G’. The gel strength and water-holding capacity showed that the higher the amount of enzyme added, the more significant the decrease in gel strength, while the gel water-holding capacity increased. In summary, the deamidation of PG and heat treatment can affect the gel properties of SPI synergistically.

Plant Protein Heat-Induced Gels: Formation Mechanisms and Regulatory Strategies

“…In addition, protein glutaminase (PG) is an enzyme that catalyses the deamidation of glutamine residues in proteins and can be used to expose hydrophobic groups and increase surface hydrophobicity. Thus, PG improves the strength of heatinduced gels [86]. According to recent research, other enzymes (alkaline proteases, papain, and trypsin) can also improve the gel properties of plant proteins.…”