Keywords: Sunflower protein, Helianthusannuus ,helianthinin, albumins, solubility, structure,denaturation, pH, temperature, ionic strength,phenoliccompounds,chlorogenicacid, foams, emulsions, functionalityThe research described in this thesis deals with the relation between specific sunflower proteins, their structure and their functional properties as a function of extrinsic factors as pH, ionic strength and temperature.Sunflower protein isolate (SI) devoid ofchlorogenicacid (CGA), the mainphenoliccompound present, was obtained withoutdenaturationof the proteins. Sunflower proteins were found to be composed of two main protein fractions: 2S albumins or sunflower albumins (SFAs) andhelianthinin. Subsequently, these protein fractions werebiochemicallyand structurally characterized under conditions relevant to food processing.Depending on pH, ionic strength, temperature and protein concentration,helianthininoccurs in the 15-18S (high molecular weight aggregate), 11 S (hexamer), 7S (trimer) or 2-3S (monomer) form. Dissociation into 7S from 11S gradually increased with increasing pH from 5.8 to 9.0. Enhancing the ionicstrengthresulted in stabilization of the 11S form. Heating and lowering the pH resulted in dissociation into themonomericform ofhelianthinin. The 11S and 7S form ofhelianthinindiffer in their secondary structure, tertiary structure, and thermal stability. With respect to solubilityas a function of pH,helianthininshows a bell shaped curve with a minimum at approximately pH 5.0 at low ionic strength. At high ionic strength,helianthininis almost insoluble at pH< 5.0.The second main sunflower fraction,SFAs, revealed to be very stable against pH changes (pH 3.0 to 9.0) and heat treatment (up to 100°C), and their solubility was only marginally affected by pH and ionic strength. The solubility of the SI as a function of pH seems to be dominated by that ofhelianthinin.Foam and emulsion properties of the sunflower isolate as well as those of purifiedhelianthinin,SFAsand combinations thereof were studied at various pH values and ionic strengths, and after heat treatment. Sunflower proteins were shown to form stable emulsions, with the exception ofSFAsat alkaline and neutral pH values. Increasing amount ofSFAsimpaired the emulsifying properties. Regarding foam properties, less foam could be formed fromhelianthininthan fromSFAs, but foam prepared withhelianthininwas more stable againstOstwaldripening and drainage than foam prepared withSFAs. Increasing amounts ofSFAshad a positive effect on foam volume and a negative one on foam stability and drainage. It was found that treatments that increase conformational flexibility improve the emulsion and foam properties of sunflower proteins.
|Qualification||Doctor of Philosophy|
|Award date||1 Dec 2003|
|Place of Publication||[S.l.]|
|Publication status||Published - 2003|
- sunflower protein
- physicochemical properties