Sunflower albumins (SFAs) are a diverse group of proteins present in sunflower isolates, with a sedimentation coefficient of approximately 2S. This research presents a detailed study of the influence of pH on the structure and solubility of SFAs. The effect of temperature on the structure of SFAs was also studied. Furthermore, the solubility of a sunflower isolate (SI) was studied and discussed in terms of its main protein components (SFAs and helianthinin). The native structure of SFAs revealed to be very stable against pH changes (pH 3.0 to 9.0) and heat treatment (>100 °C), and their solubility was only marginally affected by pH and ionic strength. The solubility of the sunflower isolate as a function of pH seems to be dominated by th...
Studies of the distribution of nitrogen, of conditions affecting its extraction and of the isolation...
Studies of the distribution of nitrogen, of conditions affecting its extraction and of the isolation...
The three-dimensional structure in aqueous solution of SFA-8, a 2S albumin 103-residue protein from ...
Sunflower albumins (SFAs) are a diverse group of proteins present in sunflower isolates, with a sedi...
Keywords: Sunflower protein, Helianthusannuus ,helianthinin, albumins, solubility, structure,denatur...
There is increasing worldwide demand for proteins of both animal and plant origin. However, animal p...
There is increasing worldwide demand for proteins of both animal and plant origin. However, animal p...
Keywords: Sunflower protein, Helianthus<span class=SpellE>annuus</span> ,<span class=SpellE>helianth...
The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was inve...
The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was inve...
The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was inve...
Foam properties of a sunflower isolate (SI), as well as those of helianthinin and sunflower albumins...
Foam properties of a sunflower isolate (SI), as well as those of helianthinin and sunflower albumins...
Emulsions were made with sunflower protein isolate (SI), helianthinin, and sunflower albumins (SFAs)...
Emulsions were made with sunflower protein isolate (SI), helianthinin, and sunflower albumins (SFAs)...
Studies of the distribution of nitrogen, of conditions affecting its extraction and of the isolation...
Studies of the distribution of nitrogen, of conditions affecting its extraction and of the isolation...
The three-dimensional structure in aqueous solution of SFA-8, a 2S albumin 103-residue protein from ...
Sunflower albumins (SFAs) are a diverse group of proteins present in sunflower isolates, with a sedi...
Keywords: Sunflower protein, Helianthusannuus ,helianthinin, albumins, solubility, structure,denatur...
There is increasing worldwide demand for proteins of both animal and plant origin. However, animal p...
There is increasing worldwide demand for proteins of both animal and plant origin. However, animal p...
Keywords: Sunflower protein, Helianthus<span class=SpellE>annuus</span> ,<span class=SpellE>helianth...
The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was inve...
The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was inve...
The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was inve...
Foam properties of a sunflower isolate (SI), as well as those of helianthinin and sunflower albumins...
Foam properties of a sunflower isolate (SI), as well as those of helianthinin and sunflower albumins...
Emulsions were made with sunflower protein isolate (SI), helianthinin, and sunflower albumins (SFAs)...
Emulsions were made with sunflower protein isolate (SI), helianthinin, and sunflower albumins (SFAs)...
Studies of the distribution of nitrogen, of conditions affecting its extraction and of the isolation...
Studies of the distribution of nitrogen, of conditions affecting its extraction and of the isolation...
The three-dimensional structure in aqueous solution of SFA-8, a 2S albumin 103-residue protein from ...