RESUMO
The aim of this study was to improve the functional properties of chickpea protein for its potential application in the food industry. The effects of low frequency high intensity ultrasound (HIU) at different power (0-300 W) and time (15-30 min) on the rheological properties, gelation, thermal stability, solubility and microstructure of chickpea protein were tested and analyzed. Based on the analysis, it was found that HIU caused the disruption of non-covalent bonds between protein chains leading to the unfolding of chickpea. The HIU-treated chickpea isolate protein aggregates were smaller and more uniformly dispersed, with increased orderly structure, thermal stability, and exposure of hydrophobic and charged groups originally buried in the interior. The experimental results also showed that the effect of HIU did not become more pronounced with increasing power and time, as the power exceeding 150 W for 30 min led to the formation of new polymers by the interactions between the exposed non-covalent groups, which were more ordered and homogeneous than those without HIU.
Assuntos
Cicer , Interações Hidrofóbicas e Hidrofílicas , Reologia , Solubilidade , Ondas UltrassônicasRESUMO
In this paper, a novel high-internal-phase Pickering emulsion (HIPPE) prepared by acid-induced self-assembly SPI gel (A/S-SPIG) was investigated. The steady-state shear test results showed that all HIPPEs were typical shear thinning emulsion, which could form stable emulsion (0.2-1.2% SPI concentration). The network structure of HIPPE stabilized by A/S-SPIG particles (0.2-1.2% SPI concentration) was continuously enhanced with increasing SPI concentration. The high concentration of SPI particles increased the crystallization temperature of the stabilized HIPPE. Meanwhile, at a concentration of 1.2%, HIPPE has the best cohesive property and stability against delamination due to weakened mobility. In conclusion, A/S-SPIG was proved excellent HIPPE stabilized particle.