Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1183138 | Food Chemistry | 2016 | 8 Pages |
•As extraction pH increased, protein yield increased but protein purity decreased.•As extraction pH increased, protein denaturation increased.•As extraction pH increased, solubility decreased from pH 3 to 4.5.•Extraction pH 8 and 9 allowed the formation of semi-solid gels upon heating.
The aim of this study was to determine the influence of extraction pH on heat-induced aggregation, gelation and microstructure of suspensions of protein isolates extracted from quinoa (Chenopodium quinoa Willd). Quinoa seed protein was extracted by alkaline treatment at various pH values (pH 8 (E8), 9 (E9), 10 (E10) and 11 (E11)), followed by acid precipitation. The obtained protein isolates were freeze dried. The protein isolates E8 and E9 resulted in a lower protein yield as well as less protein denaturation. These isolates also had a higher protein purity, more protein bands at higher molecular weights, and a higher protein solubility in the pH range of 3–4.5, compared to the isolates E10 and E11. Heating the 10% w/w protein isolate suspensions E8 and E9 led to increased aggregation, and semi-solid gels with a dense microstructure were formed. The isolate suspensions E10 and E11, on the other hand, aggregated less, did not form self-supporting gels and had loose particle arrangements. We conclude that extraction pH plays an important role in determining the functionality of quinoa protein isolates.
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