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ALPHA HELIX. B E. E. B E. BETA SHEET. Freeze dried oven dried butanol ethanol butanol ethanol. Spray dried ethanol. 0.1 mm mmmm. 0.1 mm mmmm. MAINLY HELICAL. MAINLY SHEET.
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ALPHA HELIX B E E B E BETA SHEET Freeze dried oven dried butanol ethanol butanol ethanol Spray dried ethanol
0.1 mm mmmm 0.1 mm mmmm MAINLY HELICAL MAINLY SHEET
Heat treatment during the extraction and drying process appears to cause denaturation and aggregation of kafirin, decreasing solubility. Kafirin films, where the -helical structure of the “native” protein has been retained, are better quality, smoother and more transparent, than those containing aggregated proteins with a greater -sheet content. Denatured/aggregated kafirins give less homogeneous films showing phase separation
α β a b c d e FT-IR spectra of kafirin films with sorghum condensed tannin a = unmodified film, b = 5 %, c =, 10 %, d = 15 %, e = 20 % level of modification
Tannic acid and sorghum condensed tannins stabilised the kafirin α-helical structure and decreased β-sheet formation Tannic acid cross-linking decreased the mobility of the kafirin polypeptide chains
PREDICTED VALUE RAW DATA WITH DEUTERATED GLYCEROL CORRECTED FOR MOBILE PROTEIN
GLYCEROL INCREASES THE ALPHA HELICAL CONTENT OF THE PROTEIN AND CAUSES MORE MOBILE MATERIAL TO APPEAR THAN CAN BE EXPLAINED SIMPLY BY THE AMOUNT OF PLASTICISER ADDED. Glycerol must also act as solvent
heat solvent Hydrophobic interiors unwind slightly And coagulation takes place. Degree of unwinding/ coagulation is determined by the thermal history of the sample
dry Tannin dry
Some absorption of glycerol plasticiser More plasticiser MOSTLY IMMOBILE RIGID CORE Remains alpha helical MOBILE Reverts to random coil or alpha helix Glycerol acts at as a solvent for the unwound region. Highly mobile region