Exploring the influence of different enzymes on soy hull polysaccharide emulsion stabilization: A study on interfacial behavior and structural changes
Yan Xu, Shengnan Wang, Liwen Xin, Lanxin Zhang, Lina Yang, Peng Wang, He Liu
Abstract
The interfacial behavior of soy hull polysaccharide (SHP) at the oil-water interface and the stabilization mechanism of high internal phase emulsion (HIPE) with three enzymes (α-amylase, trypsin and papain) were investigated. The diameter of the α-amylase-treated emulsion was the minimum at 40 min, indicating that the carbohydrate portions of SHP form a thick layer on the surface of the droplet to prevent aggregation. Moreover, Raman spectroscopy revealed significantly higher levels of disordered content of SHP emulsion treated with α-amylase at 60 min, potentially affecting the directional movement of SHP molecules in the emulsion. Conversely, the content of β-sheet and β-turn was lower than trypsin and papain, possibly due to ion-dipole interaction between the polar group residues within SHP and ions, or protonation with H + .