Investigation on solubility, interfacial and emulsifying properties of pumpkin (Cucurbita pepo) seed protein isolate
| Autor: | Milica Vučinić Vasić, Sandra Bučko, Ljiljana Popović, Jaroslav Katona, Žužana Vaštag, Lidija Petrović |
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| Rok vydání: | 2015 |
| Předmět: |
0303 health sciences
Chromatography biology 030309 nutrition & dietetics Chemistry Extraction (chemistry) 04 agricultural and veterinary sciences biology.organism_classification 040401 food science 6. Clean water 03 medical and health sciences Creaming Cucurbita pepo 0404 agricultural biotechnology Adsorption Isoelectric point Ionic strength Emulsion Solubility Food Science |
| Zdroj: | LWT - Food Science and Technology. 64:609-615 |
| ISSN: | 0023-6438 |
| DOI: | 10.1016/j.lwt.2015.06.054 |
| Popis: | Pumpkin (Cucurbita pepo) seed protein isolate (PSPI 1 ) with protein content of 94.3 g/100 g was obtained by alkali extraction with isoelectric precipitation. Functional properties of PSPI such as solubility, interfacial and emulsifying properties were tested as a function of pH (3–8), ionic strength (μ = 0–1 mol/dm3 NaCl) and PSPI concentration. PSPI solubility had a minimum at pH 5 and reached maximal values in alkali region at pH 8. Increase in PSPI suspension concentration led to a decrease in solubility yields at pH 3 and 8, while at pH 5 solubility yield was independent of PSPI suspension concentration. Addition of NaCl caused pronounced salting–out effect at pH 3 and slight salting–in effect at pH 5 and 8. PSPI adsorption at both air/PSPI solution and oil/PSPI solution at all pH and ionic strengths tested was evidenced by an increase in surface and interfacial pressure. Nevertheless, PSPI failed to stabilize 20% oil in water emulsions at pH 5, when phase separation occurred immediately after emulsion preparation. The most stable emulsions, regardless of ionic strength, were obtained at pH 8. All emulsions were susceptible to creaming instability. |
| Databáze: | OpenAIRE |
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