Succinylation of zein and gelatin hydrolysates improved their ice recrystallization inhibition activity.

The goal of this research was to enhance the ice recrystallization inhibition (IRI) activity of zein and gelatin hydrolysates (ZH and GH, respectively) by succinylation modification. ZH was prepared by Alcalase treatment for 3 h and then modified by succinic anhydride (SA); whereas GH was made by Alcalase hydrolysis for 0.25 h and succinylated by n-octylsuccinic anhydride (OSA). After 0.5 h of annealing at -8 °C at 40 mg/mL, modified hydrolysates decreased the average Feret's diameter of ice crystal from 50.2 μm (polyethylene glycol, negative control) to 28.8 μm (SA modified ZH) and 29.5 μm (OSA modified GH) in comparison to the unmodified hydrolysates, which had the crystal size of 47.2 μm (ZH) and 45.4 μm (GH). Also, the two succinylated samples had altered surface hydrophobicity, which potentially contributed to their enhanced IRI activity. Our results indicate that succinylation of food-derived protein hydrolysates can improve their IRI activity.