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Pumpkin seed protein isolate (PSPI) was enzymatically hydrolyzed by alcalase and pepsin to obtain H1 and H2 hydrolysates, respectively. Influence of enzymatic hydrolysis on solubility, interfacial and emulsifying properties of PSPI was investigated as a function of pH (3–8) and ionic strength (0–1 mol/dm3 NaCl). Solubility of PSPI was lowest at pI = 5. Solubility of both hydrolysates was higher than...
This study was conducted to evaluate the feasibility of pumpkin oil cake (PuOC) to form biodegradable films. The effect of heating treatment and pH of film solutions on films properties was determined. Film with the highest tensile strength (TS) (68.08MPa) and elongation to break (EB) (36.62%) was produced when pH was 12 and heating T 90°C. The same showed the best permeability properties. The total...
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