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

2016 ◽  
Vol 60 ◽  
pp. 271-278 ◽  
Author(s):  
Sandra Bučko ◽  
Jaroslav Katona ◽  
Ljiljana Popović ◽  
Lidija Petrović ◽  
Jelena Milinković
Keyword(s):  
Enzymatic Hydrolysis ◽  
Cucurbita Pepo ◽  
Seed Protein ◽  
Protein Isolate ◽  
Emulsifying Properties

scholarly journals Functional properties of pumpkin (Cucurbita pepo) seed protein isolate and hydrolysate

2016 ◽  
Vol 81 (1) ◽  
pp. 35-46 ◽  
Author(s):  
Sandra Bucko ◽  
Jaroslav Katona ◽  
Ljiljana Popovic ◽  
Zuzana Vastag ◽  
Lidija Petrovic
Keyword(s):  
Ionic Strength ◽  
Cucurbita Pepo ◽  
Seed Protein ◽  
Protein Hydrolysate ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Protein Solution ◽  
Pumpkin Seed ◽  
Solution Interface ◽  
Oil In Water

Pumpkin seed protein isolate (PSPI) was enzymatically hydrolysed by pepsin to obtain pumpkin seed protein hydrolysate, PSPH. Investigation on solubility, interfacial and emulsifying properties of both PSPI and PSPH was conducted under different conditions of pH (3-8) and ionic strength (0-1 mol/dm3 NaCl). PSPI had the lowest solubility, i.e. isoelectric point (pI), at pH 5. PSPH had higher solubility than PSPI over whole range of pH and ionic strengths tested. Decrease in surface and interfacial tension evidenced that both PSPI and PSPH adsorb at air/protein solution and oil/protein solution interface. Emulsions (20 % oil in water) stabilized by 1 g/100cm3 PSPI or PSPH solution were prepared at pH 3, 5 and 8 and ionic strength of 0 and 0.5 mol/dm3 NaCl. PSPH stabilized emulsions from coalescence at all pH and ionic strengths tested. PSPI was able to stabilize emulsions at pH 3 and 0 mol/dm3 NaCl, and at pH 8 regardless of ionic strength, while emulsions at pH 5 and both 0 and 0.5 mol/dm3 NaCl and at pH 3 when ionic strength was increased separated to oil and serum layer immediately after preparation. All emulsions were susceptible to creaming instability.

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

LWT ◽  
2015 ◽  
Vol 64 (2) ◽  
pp. 609-615 ◽  
Author(s):  
Sandra Bučko ◽  
Jaroslav Katona ◽  
Ljiljana Popović ◽  
Žužana Vaštag ◽  
Lidija Petrović ◽  
...  
Keyword(s):  
Cucurbita Pepo ◽  
Seed Protein ◽  
Protein Isolate ◽  
Emulsifying Properties

The Influence of Enzymatic Hydrolysis on Adsorption and Interfacial Dilatational Properties of Pumpkin (Cucurbita pepo) Seed Protein Isolate

2018 ◽  
Vol 13 (3) ◽  
pp. 217-225
Author(s):  
Sandra Bučko ◽  
Jaroslav Katona ◽  
Lidija Petrović ◽  
Jelena Milinković ◽  
Ljiljana Spasojević ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Cucurbita Pepo ◽  
Seed Protein ◽  
Protein Isolate

Influence of enzymatic hydrolysis, pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

2018 ◽  
Vol 53 (10) ◽  
pp. 2316-2324 ◽  
Author(s):  
Adeola M. Alashi ◽  
Christopher L. Blanchard ◽  
Rodney J. Mailer ◽  
Samson O. Agboola ◽  
John A. Mawson ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Storage Temperature ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Canola Protein ◽  
And Storage ◽  
Canola Protein Isolate

scholarly journals An investigation on the influence of pH and ionic strength on the adsorption and interfacial dilatational properties at the oil-water interface of pumpkin (Cucurbita pepo) seed protein hydrolysate

2018 ◽  
Vol 83 (7-8) ◽  
pp. 847-861
Author(s):  
Sandra Bucko ◽  
Jaroslav Katona ◽  
Lidija Petrovic ◽  
Jelena Milinkovic ◽  
Jadranka Fraj ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Rate Constant ◽  
Cucurbita Pepo ◽  
Seed Protein ◽  
Protein Hydrolysate ◽  
Protein Isolate ◽  
Pumpkin Seed ◽  
Interfacial Pressure ◽  
Oscillation Frequencies ◽  
Influence Of Ph

Pumpkin (Cucurbita pepo) seed protein hydrolysate (PSPH) was obtained by enzymatic hydrolysis of pumpkin seed protein isolate using pepsin. Influence of pH (3, 5 and 8) and ionic strength, Ic (0?1 mol dm-3), on the adsorption kinetics of PSPH (diffusion rate constant, kdiff, and adsorption rate constant, kads), interfacial pressure (?) and interfacial dilatational properties (dilatational elasticity, E?, and viscosity, E?) of the oil?PSPH solution interfaces was investigated at different PSPH concentrations (c = 0.0014?14 g dm-3). It was found that PSPH adsorbs to the interface at c ? 0.0014 g dm-3, regardless of pH and ionic strength, as evidenced by the increase in interfacial pressure. The kdiff and kads value were found to be the highest at pH 3 and the lowest at pH 5 at the corresponding concentrations. The dilatational properties of the interfaces, which were investigated at different oscillation frequencies, ?, 0.01?0.2 Hz, showed that the E? of the oil?PSPH solution interfaces is much higher than its E?. Moreover, E? increases with increasing PSPH concentration at pH 5 and 8, and with increasing Ic, regardless of the pH, while E? changes only minimally.

scholarly journals Fabrication of Oil-in-Water Emulsions with Whey Protein Isolate–Puerarin Composites: Environmental Stability and Interfacial Behavior

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 705
Author(s):  
Yejun Zhong ◽  
Jincheng Zhao ◽  
Taotao Dai ◽  
Jiangping Ye ◽  
Jianyong Wu ◽  
...  
Keyword(s):  
Interfacial Tension ◽  
Whey Protein ◽  
Surface Protein ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Environmental Stability ◽  
Dependent Manner ◽  
Emulsifying Properties ◽  
Interfacial Behavior ◽  
Concentration Dependent Manner

Protein–polyphenol interactions influence emulsifying properties in both directions. Puerarin (PUE) is an isoflavone that can promote the formation of heat-set gels with whey protein isolate (WPI) through hydrogen bonding. We examined whether PUE improves the emulsifying properties of WPI and the stabilities of the emulsions. We found that forming composites with PUE improves the emulsifying properties of WPI in a concentration-dependent manner. The optimal concentration is 0.5%, which is the highest PUE concentration that can be solubilized in water. The PUE not only decreased the droplet size of the emulsions, but also increased the surface charge by forming composites with the WPI. A 21 day storage test also showed that the maximum PUE concentration improved the emulsion stability the most. A PUE concentration of 0.5% improved the stability of the WPI emulsions against environmental stress, especially thermal treatment. Surface protein loads indicated more protein was adsorbed to the oil droplets, resulting in less interfacial WPI concentration due to an increase in specific surface areas. The use of PUE also decreased the interfacial tension of WPI at the oil–water interface. To conclude, PUE improves the emulsifying activity, storage, and environmental stability of WPI emulsions. This result might be related to the decreased interfacial tension of WPI–PUE composites.

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