Thermal properties of globulin from rice (Oryza sativa) seeds

Thermal Characterization and Phase Behavior of a Ready-to-Eat Breakfast Cereal Formulation and its Starchy Components

“…Denaturation temperatures (or peak maximum temperature) in rice flour proteins of 73, 79, and 82°C were reported by Ju et al 32 , for albumin, globulin, and glutelin, respectively. Ellepola and Ma 33 , reported denaturation temperatures of 97.6 and 98.5°C for crude and purified rice globulin, which are close to the peak temperature of the rice flour presented in Table 4. Although the denaturation temperature of the protein fraction can vary depending on the extraction method, the bimodal transition obtained at lower temperature (58.8-79.6°C) for rice flour (Figure 2), suggests that it could then be related to the starch gelatinization and one or two protein fraction denaturation (probably albumin and globulin), occurring sequentially as reported to occur in rice flour at a peak temperature of 80.5°C by Ju et al 32 ; and the second peak may then be related to the other rice protein fraction denaturation.…”

“…However, this contribution can also come from amorphous amylose-lipid complexes that dissociate at temperature lower than 100°C and can be present in native cereal materials 27,35 . Enthalpy values reported in Table 4 are within those reported for protein denaturation in rice and oat products (including protein fractions and flours), which vary from 6 to 26 J/g 30,33,36 . The values characterizing the third transition in Figure 2, are shown in Table 5.…”

The effect of sodium chloride on microstructure, water migration, and texture of rice noodle

“…This indicated that the presence of NaCl enhanced the network forming protein. Ellepola and Ma (2006) reported that the addition of NaCl influences the electrostatic interaction of charged and polar groups of rice globulin and also modifies the hydrophobic interactions. Therefore, in the presence of NaCl in rice noodle, the rice protein molecules may be in the form of charged molecules and the charged protein molecules may affect the cross linkage and the protein network formation.…”

Study of thermal properties and heat-induced denaturation and aggregation of soy proteins by modulated differential scanning calorimetry

“…Differential scanning calorimetry (DSC) has been widely used to characterize the thermal properties of food proteins, including heat-induced denaturation [1][2][3][4][5][6] and glass transition [7][8][9]. However, the DSC technique suffers from limitations with respect to its ability to describe complex transitions and individual contributing components.…”