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

<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>

2021 ◽  
Vol 22 (12) ◽  
pp. 6592
Author(s):  
Artur Seweryn ◽  
Tomasz Wasilewski ◽  
Anita Bocho-Janiszewska

The article shows that the type and concentration of inorganic salt can be translated into the structure of the bulk phase and the performance properties of ecological all-purpose cleaners (APC). A base APC formulation was developed. Thereafter, two types of salt (sodium chloride and magnesium chloride) were added at various concentrations to obtain different structures in the bulk phase. The salt addition resulted in the formation of spherical micelles and—upon addition of more electrolyte—of aggregates having a lamellar structure. The formulations had constant viscosities (ab. 500 mPa·s), comparable to those of commercial products. Essential physical-chemical and performance properties of the four formulations varying in salt types and concentrations were evaluated. It was found that the addition of magnesium salt resulted in more favorable characteristics due to the surface activity of the formulations, which translated into adequately high wettability of the investigated hydrophobic surfaces, and their ability to emulsify fat. A decreasing relationship was observed in foaming properties: higher salt concentrations lead to worse foaming properties and foam stability of the solutions. For the magnesium chloride composition, the effect was significantly more pronounced, as compared to the sodium chloride-based formulations. As far as safety of use is concerned, the formulations in which magnesium salt was used caused a much lesser irritation compared with the other investigated formulations. The zein value was observed to decrease with increasing concentrations of the given type of salt in the composition.


1960 ◽  
Vol 6 (5) ◽  
pp. 535-543 ◽  
Author(s):  
Dinah Abram ◽  
N. E. Gibbons

The optical densities of suspensions of cells of Halobacterium cutirubrum, H. halobium, or H. salinarium, grown in media containing 4.5 M sodium chloride, increase as the salt concentration of the suspending medium decreases, until a maximum is reached at about 2 M; below this concentration there is an abrupt decrease in optical density. The cells are rod shaped in 4.5 M salt and change, as the salt concentration decreases, through irregular transition forms to spheres; equal numbers of transition forms and spheres are present at the point of maximum turbidity, while spheres predominate at lower salt concentrations. Cells suspended in 3.0 M salt, although slightly swollen, are viable, but viability decreases rapidly with the more drastic changes in morphology at lower salt concentrations. Cells grown in the presence of iron are more resistant to morphological changes but follow the same sequence. Cells "fixed" with formaldehyde, at any point in the sequence, act as osmometers and do not rupture in distilled water although their volume increases 10–14 times. The results indicate that the red halophilic rods require a high sodium chloride content in their growth or suspending medium to maintain a rigid cell wall structure.


2020 ◽  
Vol 27 (1) ◽  
pp. 3-12
Author(s):  
Prasanth KS Pillai ◽  
Yulinglong Ouyang ◽  
Andrea K Stone ◽  
Michael T Nickerson

This research examines changes to the functional (solubility, emulsifying and foaming) properties of pea protein isolate when complexed with commercial citrus pectin of different structural attributes. Specifically, a high methoxy (P90; degree of esterification: 90.0%; degree of blockiness: 64.5%; galacturonic acid content 11.4%) and low methoxy (P29; degree of esterification: 28.6%; degree of blockiness: 31.1%; galacturonic acid: 70%) pectin at their optimum mixing ratios with pea protein isolate (4:1 pea protein isolate to P90; 10:1 pea protein isolate to P29) were assessed at the pHs associated with critical structure forming events during the complexation process (soluble complexation (pHc), pH 6.7 and 6.1; insoluble complex formation (pHϕ1), pH 4.0 and 5.0; maximum complexation (pHopt), pH 3.5 and 3.8; dissolution of complexes, pH 2.4 and 2.1; for admixtures of pea protein isolate–P90 and pea protein isolate–P29, respectively). Pea protein isolate solubility was improved from 41 to 73% by the presence of P90 at pH 6.0 and was also moderately increased at pH 4.0 and pH 5.0 by P90 and P29, respectively. The emulsion stability of both pea protein isolate–pectin complexes was higher than the homogeneous pea protein isolate at all critical pHs except pHopt as well as pHc for pea protein isolate–P29 only. P90, with the higher level blockiness and esterification, displayed better foaming properties at the maximal complexation pH when complexed with pea protein isolate than pea protein isolate–P29 or pea protein isolate alone. However at pHϕ2, pea protein isolate–P29 admixtures produced foams with 100% stability, increasing pea protein isolate foam stability by 85%. The enhanced functionality of pea protein isolate–pectin complexes based on the type of pectin used at critical pHs indicates they may be useful biopolymer ingredients in plant protein applications.


2010 ◽  
Vol 16 (5) ◽  
pp. 451-458 ◽  
Author(s):  
J.G. Rocha-Estrada ◽  
J.H. Córdova-Murueta ◽  
F.L. García-Carreno

Functional properties of protein from mantle and fin of the jumbo squid Dosidicus gigas were explained based on microscopic muscle fiber and protein fractions profiles as observed in SDS-PAGE. Fin has higher content of connective tissue and complex fiber arrangement, and we observed higher hardness of fin gels as expected. Myosin heavy chain (MHC) was found in sarcoplasmic, myofibril and soluble-in-alkali fractions of mantle and only in sarcoplasmic and soluble-in-alkali fractions of fin. An additive effect of salt concentration and pH affected the solubility and foaming properties. Fin and mantle proteins yielded similar results in solubility tests, but significant differences occurred for specific pH and concentrations of salt. Foaming capacity was proportional to solubility; foam stability was also affected by pH and salt concentration. Hardness and fracture strength of fin gels were significantly higher than mantle gels; gels from proteins of both tissues reached the highest level in the folding test. Structural and molecular properties, such as MHC and paramyosin solubility, arrangement of muscle fibers and the content of connective tissue were useful to explain the differences observed in these protein properties. High-strength gels can be formed from squid mantle or fin muscle. Fin displayed similar or better properties than mantle in all tests.


Foods ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2238
Author(s):  
Xin Li ◽  
Yue-Meng Wang ◽  
Cheng-Feng Sun ◽  
Jian-Hao Lv ◽  
Yan-Jun Yang

As an excellent foaming agent, egg white protein (EWP) is always contaminated by egg yolk in the industrial processing, therefore, decreasing its foaming properties. The aim of this study was to simulate the industrial EWP (egg white protein with 0.5% w/w of egg yolk) and characterize their foaming and structural properties when hydrolyzed by two types of esterase (lipase and phospholipase A2). Results showed that egg yolk plasma might have been the main fraction, which led to the poor foaming properties of the contaminated egg white protein compared with egg yolk granules. After hydrolyzation, both foamability and foam stability of investigated systems thereof (egg white protein with egg yolk, egg white protein with egg yolk plasma, and egg white protein with egg yolk granules) increased significantly compared with unhydrolyzed ones. However, phospholipids A2 (PLP) seemed to be more effective on increasing their foaming properties as compared to those systems hydrolyzed by lipase (LP). The schematic diagrams of yolk fractions were proposed to explain the aggregation and dispersed behavior exposed in their changes of structures after hydrolysis, suggesting the aggregated effects of LP on yolk plasma and destructive effects of PLP on yolk granules, which may directly influence their foaming properties.


2017 ◽  
Vol 35 (No. 1) ◽  
pp. 57-66 ◽  
Author(s):  
Pan Mingzhe ◽  
Meng Xianjun ◽  
Jiang Lianzhou ◽  
Yu Dianyu ◽  
Liu Tianyi

Effect of polyols (mannitol, sorbitol, and xylitol) at three concentrations (5, 10, and 15% w/w) on the structure of soy protein isolates (SPI) was investigated. Changes in foaming properties of SPI were then examined with the addition of polyols at different concentrations. The interactions between SPI and polyols resulted in a substantial decrease in protein surface hydrophobicity and intrinsic tryptophan fluorescence intensity, along with the covering of tyrosine. Furthermore, circular dichroism (CD) spectroscopy of SPI suggested that a more ordered and compact conformation was induced by polyols. Consequently, these structural changes led to lower foamability of SPI. An increase in the viscosity of SPI suspension seemed to be advantageous for improving the foam stability of SPI.


2016 ◽  
Vol 41 (4) ◽  
pp. e13073 ◽  
Author(s):  
Toan Thuc Pham ◽  
Thi Thu Tra Tran ◽  
Nu Minh Nguyet Ton ◽  
Van Viet Man Le

2016 ◽  
Vol 81 (1) ◽  
pp. 35-46 ◽  
Author(s):  
Sandra Bucko ◽  
Jaroslav Katona ◽  
Ljiljana Popovic ◽  
Zuzana Vastag ◽  
Lidija Petrovic

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.


Author(s):  
Dávid Nagy ◽  
Viktória Zsom-Muha ◽  
Csaba Németh ◽  
József Felföldi

AbstractThe aim of this study was to determine the effect of ultrasound treatment on foaming properties of egg white. The samples were sonicated at 20/40 kHz and 180/300 W equipment power (3.7/6.9 W absorbed power) for 30, 45 and 60 minutes. Foam capacity had been increased by 25% due to sonication at 40 kHz and 6.9 W absorbed power for 60 minutes. This phenomenon may be caused by the homogenization effect of ultrasound and protein exposure of hydrophobic groups that improve the adsorption of protein onto the air/water interfacial molecules. It is found that frequency and duration of the treatment have no significant impact on the changes in foam capacity, only the absorbed power. On the other hand, foam stability had been decreased during the ultrasonic treatment. We can assume that sonication decreases the potential difference between the dispersed particles and the dispersion medium and this may be the cause of the collapse of the foam structure due to ultrasound treatment. In this case frequency, treatment time, and the absorbed power had a significant effect on the stability.


1961 ◽  
Vol 7 (4) ◽  
pp. 483-489 ◽  
Author(s):  
N. E. Gibbons ◽  
John I. Payne

The red halophiles, Halobacterium salinarium, H. cutirubrum, H. halobium, and Sarcina litoralis, grew most rapidly at salt concentrations of 20–25% and temperatures of 40–45 °C. Maximum turbidity was obtained at similar salt concentrations but at 35–40 °C. An unidentified colorless rod grew most rapidly at salt concentrations of 17.5–20% and temperatures of 40–50 °C, but produced maximum yield at 30 °C. The rod forms changed from long slender rods through irregular shapes to spheres as the salt concentration was decreased. At temperatures above the optimum, cells were very irregular, but otherwise temperature at any one salt concentration had little or no effect on the morphology.


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