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.

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.

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

scholarly journals Optimization of the Emulsifying Properties of Food Protein Hydrolysates for the Production of Fish Oil-in-Water Emulsions

Foods ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 636 ◽  
Author(s):  
Marta Padial-Domínguez ◽  
F. Javier Espejo-Carpio ◽  
Raúl Pérez-Gálvez ◽  
Antonio Guadix ◽  
Emilia M. Guadix
Keyword(s):  
Fish Oil ◽  
Soy Protein ◽  
Protein Hydrolysate ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Degree Of Hydrolysis ◽  
Emulsifying Properties ◽  
Oil In Water ◽  
Soy Protein Hydrolysate

The incorporation of lipid ingredients into food matrices presents a main drawback—their susceptibility to oxidation—which is associated with the loss of nutritional properties and the generation of undesirable flavors and odors. Oil-in-water emulsions are able to stabilize and protect lipid compounds from oxidation. Driven by consumers’ demand, the search for natural emulsifiers, such as proteins, is gaining much interest in food industries. This paper evaluates the in vitro emulsifying properties of protein hydrolysates from animal (whey protein concentrate) and vegetal origin (a soy protein isolate). By means of statistical modelling and bi-objective optimization, the experimental variables, namely, the protein source, enzyme (i.e., subtilisin, trypsin), degree of hydrolysis (2–14%) and emulsion pH (2–8), were optimized to obtain their maximal in vitro emulsifying properties. This procedure concluded that the emulsion prepared from the soy protein hydrolysate (degree of hydrolysis (DH) 6.5%, trypsin) at pH 8 presented an optimal combination of emulsifying properties (i.e., the emulsifying activity index and emulsifying stability index). For validation purposes, a fish oil-in-water emulsion was prepared under optimal conditions, evaluating its physical and oxidative stability for ten days of storage. This study confirmed that the use of soy protein hydrolysate as an emulsifier stabilized the droplet size distribution and retarded lipid oxidation within the storage period, compared to the use of a non-hydrolyzed soy protein isolate.

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 Effect of Xanthan and Arabic Gums on Foaming Properties of Pumpkin (Cucurbita pepo) Seed Protein Isolate

2013 ◽  
Vol 3 (1) ◽  
pp. 87 ◽  
Author(s):  
Quirino Dawa ◽  
Yufei Hua ◽  
Moses Vernonxious Madalitso Chamba ◽  
Kingsley George Masamba ◽  
Caimeng Zhang
Keyword(s):  
Sodium Chloride ◽  
Salt Concentration ◽  
Seed Protein ◽  
Foam Stability ◽  
Chloride Concentration ◽  
Egg White ◽  
Protein Isolate ◽  
Foaming Properties ◽  
Ph Optimum ◽  
Pumpkin Seed

<p>Understanding how foaming properties of proteins are affected by factors such as pH, salt concentration and temperature is essential in predicting their performance and utilisation. In this study, the effects of pH and salt concentration were studied on the foaming properties of pumpkin seed protein isolate (PSPI) and PSPI- xanthan (XG)/Arabic (GA) gum blends. The foaming properties of the PSPI-GA/XG blends were also compared with egg white. Foam stability (FS) was significantly affected by pH with PSPI: GA (25:4) and PSPI: XG (25:1) having a significantly higher stability at pH 2 with the lowest foam stability at pH 4. Sodium chloride (0.2-1.0 M) did not significantly affect foaming properties although PSPI: GA (25:4) had the highest FC (89.33 ± 3.24%) and FS (76.83 ± 1.53 min) at 0.2 M sodium chloride concentration. The foaming capacity (FC) of PSPI: GA (25:4) blend (128.00 ± 0.91%) was significantly higher (<em>p </em><em>&lt; </em>0<em>.</em>05) than that of egg white (74.00 ± 1.33%) but its FS was significantly lower. It was further revealed that the FC of egg white (74.00 ± 1.33%) was comparable to the PSPI:XG (25:1) blend (74.00 ± 1.46%) but the FS for egg white (480.00 ± 2.67 min) was significantly higher (<em>p </em><em>&lt; </em>0<em>.</em>05) than the FS (116.21 ± 0.86 min) of PSPI:XG (25:1). The foaming properties of PSPI and PSPI-xanthan (XG)/Arabic (GA) blends were significantly affected by pH. Optimum foaming properties, PSPI:XG (25:1) and PSPI:GA (25:4) were observed at pH 2 and heat treatment temperature of 80 ºC.</p>

Fabrication and emulsifying properties of non-covalent complexes between soy protein isolate fibrils and soy soluble polysaccharides

2021 ◽  
Author(s):  
Hekai Zhao ◽  
Shengnan Wang ◽  
Guilan Zhao ◽  
Yangyang Li ◽  
Xiulin Liu ◽  
...  
Keyword(s):  
Ir Spectroscopy ◽  
Zeta Potential ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Oil In Water ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Non-covalent complexes (SPIF/SSPS) between soy protein isolate fibrils (SPIF) and soy soluble polysaccharides (SSPS) were fabricated and used to stabilize oil-in-water (O/W) emulsions. FT-IR spectroscopy and zeta potential results demonstrated...

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