Investigating the functionality of enzymatically (transglutaminase and alcalase) treated almond protein isolate

The effects of partial hydrolysis on the functional properties of almond protein isolate (API) were investigated by treating the isolate with alcalase enzyme (2.4U/g) and a subsequent polymerization of API was studied using the enzyme, transglutaminase (121U/g). The result obtained showed that partial hydrolysis could induce structural changes in almond protein, mainly reflecting at the molecular weight, duration of hydrolysis, and the active site of the enzymes. On comparing the two enzymes' ability to react on API, enzyme alcalase resulted in producing hydrolysates with the highest protein solubility of 89.38%, surface hydrophobicity of 62.68, and foaming expansion of 31% at the 60th minute of hydrolysis and produced lower molecular weight peptides. Although alcalase API hydrolysates improved the protein's functionality, the enzyme failed to increase the substrate's emulsion and foaming stabilities. On the other hand, transglutaminase enzyme produced higher molecular weight peptides and excelled in enhancing the stability of emulsion and foam along with the elevation of % degree of hydrolysis.

Automated summary

This study investigated the effects of partial hydrolysis on the functional properties of almond protein isolate (API). Alcalase enzyme resulted in hydrolysates with high protein solubility, hydrophobicity, and foaming expansion, while transglutaminase enzyme produced high molecular weight peptides and improved emulsion and foam stability.