Study on Conformation and Functional Properties of Walnut Protein and its Components
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Abstract:
The physicochemical and functional properties of walnut protein and its main components (glutelin and globulin) were examined. Walnut protein had a higher denaturation temperature (Td=104.42 ℃) and higher enthalpy (ΔH=12.93 J/g) than glutelin and globulin (p<0.05), with higher cooperativity of thermal transition. Walnut protein had the lowest sulfhydryl content while globulin had the highest. Most sulfhydryl groups of walnut protein were embedded within the molecule and it had the highest content of disulfide bonds (5.2 μmol/g), while those of glutelin and globulin were mostly exposed on the surface. The fluorescence results indicated that walnut protein had a dense tertiary structure, while that of globulin was relatively looser. The descending order of surface hydrophobicity of the three proteins was glutelin, walnut protein, and globulin. The emulsifying stability of walnut protein was the strongest among the three, owing to its compact structure and high disulfide content, whereas glutelin exhibited the worst emulsifying stability. Globulin had a loose structure with more active sites, exhibiting greater gel properties than walnut protein and glutelin.
