Contact
    Start Publications Investigation on solubility, interfacial and emulsifying ...
    ←  Publication Finder
    Attension

    Investigation on solubility, interfacial and emulsifying properties of pumpkin (Cucurbita pepo) seed protein isolate

    Year: 2015

    Journal: LWT-FOOD SCIENCE AND TECHNOLOGY, Vol. 64, p 609-615, 20170208

    Authors: Bucko, Sandra; Katona, Jaroslav; Popovic, Ljiljana; Vastag, Zuzana; Petrovic, Lidija; Vucinic-Vasic, Milica

    Organizations: Univ Novi Sad, Fac Technol, Novi Sad 21000, Serbia; Univ Novi Sad, Fac Tech Sci, Novi Sad 21000, Serbia

    Pumpkin (Cucurbita pepo) seed protein isolate (PSPI1) 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 (mu = 0-1 mol/dm(3) 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. (C) 2015 Elsevier Ltd. All rights reserved.