Complexation between curcumin and walnut protein isolate modified by pH shifting combined with protein-glutaminase

The poor techno-functional properties of walnut protein isolate (WPI) limit its application as carrier to improve bioavailability of curcumin. In this study, WPI was modified by pH-shifting (PS) and protein-glutaminase (PG). Changes on the physicochemical and structural characteristics of WPI and effects on complexation with curcumin were investigated. Treatment of PS plus PG increased electrostatic repulsion of WPI with altered secondary and tertiary structure. Solubility of WPI was greatly improved from 18.09% to 52.90%. The increased flexibility resulted in reduced particle size and increased exposure of hydrophobic groups. The improved amphiphilicity of WPI provided more binding sites for complexation with curcumin. Encapsulation efficiency of curcumin was increased from 32.50% to 94.48%. Interestingly, the formed complexes were able to protect curcumin from degradation with improved storage stability and bioaccessibility. Thus, PS plus PG could serve as effective modification strategy for utilization of WPI as a promising delivery vehicle for hydrophobic bioactives.