Effect of barley antifreeze protein on thermal properties and water state of dough during freezing and freeze-thaw cycles

Peanut protein isolate (PPI) solutions were modified by dielectric barrier discharge (DBD) cold plasma (CP) treatment. Effects of CP treatment on the solubility, emulsion stability, and water holding capacity (WHC) of peanut protein were studied. The results showed a significant improvement in solubility, emulsion stability, and WHC following CP treatment. CP treatment resulted in the unfolding of PPI structure, thereby increasing the β-sheet and random coil content and decreasing the α-helix and β-turn content, as analyzed by Fourier-transform infrared spectroscopy. Low-field nuclear magnetic resonance showed an increase in the peak area of T
 21 relaxation time by CP treatment and the change in T
 21 peak area was in agreement with the result of WHC. This study demonstrated that CP may be successfully applied as a method to modify the functionality of PPI.

Effects of Dielectric Barrier Discharge (DBD) Cold Plasma Treatment on Physicochemical and Functional Properties of Peanut Protein

Ice structuring proteins from plants: Mechanism of action and food application

The effects of heat treatment on soymilk protein denaturation were studied by differential scanning calorimetry (DSC) and electrophoresis. Transition behavior of soymilk was studied by DSC. Three endotherms were found in DSC heating curves; the transition observed at around 70°C is attributed to the denaturation of 7S (b-conglycinin) and the transition at around 90°C is to 11S (glycinin). The denaturation temperature increased with the increasing soymilk protein content. The change of electrophoretic patterns after heat treatments indicated that soy proteins were dissociated into subunits, some of which coalesced. When the heating temperature is below their denaturation temperature, the protein fractions cannot completely be denatured even after heat exposure for extended periods of time.

DSC and electrophoretic studies on soymilk protein denaturation

Polycarboxylates enhance beetle antifreeze protein activity.

Antifreeze protein (AFP) can lower the freezing point by inhibiting the growth of ice crystals. In this article, the thermal hysteresis activity (THA) of a plant AFP was measured with differential scanning calorimetry (DSC). As is shown, when the amount of ice in the sample was less than 5% THA of this AFP reached as high as 0.35°C. The secondary structure of this AFP was studied with circular dichroism (CD). The CD spectrum from 195to 240 nm indicated a well-defined secondary structure consisting 11% α-helix, 34%antiparallel β-sheet and 55% random coil.

Differential Scanning Calorimetric and Circular Dichroistic Studies on Plant Antifreeze Proteins

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Differential Scanning Calorimetric and Circular Dichroistic Studies on Plant Antifreeze Proteins