The effect of enzymatic deamidation on the solubility and emulsifying properties of walnut protein isolate

Alkaline-extracted walnut protein isolates (WPI) exhibit limited solubility, which poses challenges for their application in the food industry. The present study investigated the effects of protein-glutaminase (PG) deamidation on the physicochemical characteristics, solubility and emulsifying properties of WPI.

The deamidation process of WPI was monitored by assessing the release of free ammonia and the reduction in solution turbidity. PG deamidation significantly increased the surface charge of WPI and modified its surface hydrophobicity with increasing deamidation degree (DD), resulting in a gradual improvement in solubility by approximately 50-70%. Furthermore, the emulsifying capacity of deamidated WPI (DeWPI), specifically at 0.25 h (DeWPI0.25, DD 7%) and 9 h (DeWPI9, DD 23%), was evaluated for stabilizing low internal phase emulsions (LIPEs) and high internal phase emulsions (HIPEs). LIPEs stabilized by WPI and DeWPI0.25 exhibited significant flocculation of oil droplets, leading to decreased stability against heat, salt treatment and storage compared to those stabilized by DeWPI9. DeWPI-stabilized HIPEs showed a 2-2.5-fold higher storage modulus compared to those stabilized by WPI. However, HIPEs stabilized by DeWPI0.25 displayed higher flow stress and flow strain compared to DeWPI9-stabilized HIPEs. Overall, DeWPI-stabilized HIPEs demonstrated relatively high physical stability against storage, heat treatment and high ionic strength.

PG deamidation significantly enhanced the solubility and influenced the emulsifying properties of WPI in a manner dependent on the DD. © 2024 Society of Chemical Industry.