Anais do Simpósio Latino Americano de Ciências de Alimentos
Anais do 14 SLACA - Simpósio Latino Americano de Ciência de Alimentos

Gelatin peptides have potential to inhibit ice recrystallization (IIR) in foods. In this context, the work aimed to hydrolyze gelatin and evaluate its IIR potential. Central composite design was used to optimize the temperature (39.5, 46 and 52.5 °C) and time (18, 34 and 50 min) used for gelatin hydrolysis. Pepsin and substrate ratio was 1:50. The gelatin solution was prepared by dissolving 1.65 g in 6.6 ml deionized water at pH 2.0. After hydrolysis, the solutions were boiled for 10 min, cooled and centrifuged at 4677xg for 40 min. Supernatants were evaluated for IIR capacity. 10 μL of 30% (w/w) sucrose solution, 10 μL of hydrolysate and 10 μL of iso-amyl alcohol (98.5%) were added to the glass slides. The slides were frozen at −75 °C for 10 min, then the temperature was intercalated between -18 and -8 °C at a rate of 1 cycle for 15 min, being performed 3 cycles. Subsequently, the samples were observed under an optical microscope (40x magnification) and the size of the ice crystals before and after the cycles were measured using ImageJ software. For each treatment, 50 measurements were taken and the variation in diameters was analyzed using the Statistica software. The treatments presented significant differences (p<0.05) and a model (R² = 0.988) was adjusted containing the factors temperature, time, and the interaction between them. Before the thermal cycles the size of the crystals ranged from 0.0621 to 0.0740 mm and after the cycles it ranged from 0.0624 to 0.1395 mm. Slides produced with protein hydrolysates from hydrolysis at high temperature (52.5 °C) showed higher IIR potential, and probably this condition favored enzyme-substrate reactivity. Therefore, it was observed that gelatin protein hydrolysates have a good capacity as IIR.