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Effects of thermal treatment on structure and surface hydrophobicity of sunflower seed protein isolate |
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DOI: |
KeyWord:sunflower seed protein isolate thermal treatment aggregate structure surface hydrophobicity |
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Abstract: |
With untreated sunflower seed protein isolate (SSPI) as control,7% SSPI suspension was respectively heated at 92,102?℃ (denaturation temperature) and 112?℃ for 10 min to study the effects of thermal treatment on structure and surface hydrophobicity of SSPI. The results showed that thermal treatment induced a significant change in SSPI subunits content and formation of aggregates; the surface appearance of thermal treated SSPI was rough,loose and porous,and its microstructure was more irregular; after thermal treatment,protein molecules streched,SSPI aggregated,and relative fluorescence intensity and surface hydrophobicity of SSPI decreased. |
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