Protein solubility in water is a key property of food proteins. The aim of this work was to study the solubility and microstructural properties as a function of pH of… Click to show full abstract
Protein solubility in water is a key property of food proteins. The aim of this work was to study the solubility and microstructural properties as a function of pH of both protein fractions (water-soluble (WSPE) and water-insoluble protein extracts (WISPE)) obtained from the microalga Chlorella protothecoides, which is promising for food use. Protein solubility was determined as the ratio of protein concentration in the supernatant after centrifugation to total protein concentration. An unusually high solubility and only slight gravitational separation across a very broad pH-range (2-12) were observed for the WSPE with a minimum protein solubility of 84.3 ± 2.2% at pH 2. The origin of this high pH-independent protein solubility was attributed to a high degree of glycosylation and a high amount of hydrophilic amino acids. In contrast, the WISPE was found to contain strongly aggregated proteins, and these large aggregates separated rapidly from solution by gravitation independent of the pH. This corresponded to their protein solubility, which was overall low in the pH-range of 2-11, and only increased at pH 12 to a maximum solubility of 26.9 ± 2.8%. These results suggest that the WSPE of Chlorella protothecoides may exhibit unique properties for food formulations, allowing for example for both acidified, neutral or slightly alkaline foods to be formulated, whereas WISPE may be more suited for foods where phase separation is rather slow.
               
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