Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1

Bolontrade, Agustín Juan; Scilingo, Adriana Alicia; Añón, Marı́a Cristina

doi:10.1016/j.colsurfb.2012.12.039

Cited by 37 publications

(42 citation statements)

References 26 publications

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“…The ionic strength (IS) was adjusted to 0.5 and 0.06 with 0.5 M NaCl, obtaining four amaranth isolates named AI pH2-highIS, AI pH8-highIS, AI pH2-lowIS and AI pH8-lowIS [9].…”

Section: Preparation Of Amaranth Isolatesmentioning

confidence: 99%

“…Recently, we have studied interfacial properties of amaranth proteins. In particular [9], we studied the diffusion, adsorption and rearrangement phenomena occurring at the air-water interface, the relation between these phenomena and the protein structure and the influence of these factors in the formation of foams formulated with them. We have found that the acidic pH (treatment at pH 2, together with the increase of ionic strength) favours adsorption of proteins, reduces the time for a rearrangement and improves the foaming properties increasing foaming capacity and forming more dense and homogeneous foams [9].…”

Section: Introductionmentioning

confidence: 99%

“…In particular [9], we studied the diffusion, adsorption and rearrangement phenomena occurring at the air-water interface, the relation between these phenomena and the protein structure and the influence of these factors in the formation of foams formulated with them. We have found that the acidic pH (treatment at pH 2, together with the increase of ionic strength) favours adsorption of proteins, reduces the time for a rearrangement and improves the foaming properties increasing foaming capacity and forming more dense and homogeneous foams [9]. The aim of this work was study the capability of amaranth proteins to stabilize foams under different pH and ionic strength conditions analysing the rheological behaviour of air-water interface; with the final objective of using the amaranth proteins in foam type-products.…”

Section: Introductionmentioning

confidence: 99%

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Amaranth proteins foaming properties: Film rheology and foam stability – Part 2

Bolontrade

Scilingo

Añón

2016

Colloids and Surfaces B: Biointerfaces

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In this work the influence of pH and ionic strength on the stability of foams prepared with amaranth protein isolate was analyzed. The behaviour observed was related to the physico-chemical and structural changes undergone by amaranth protein as a result of those treatments. The results obtained show that foams prepared at acidic pH were more stable than the corresponding to alkaline pH. At pH 2.0 the foams presented higher times and more volumes of drainage. This behaviour is consistent with the characteristics of the interfacial film, which showed a higher viscoelasticity and a greater flexibility at acidic pH than alkaline pH value, which in turn increased by increasing the concentration of proteins in the foaming solution. It is also important to note that the presence of insoluble protein is not necessarily detrimental to the properties of the foam. Detected changes in the characteristics of the interfacial film as in the foam stability have been attributed to the increased unfolding, greater flexibility and net charge of amaranth proteins at acidic conditions.

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“…The ionic strength (IS) was adjusted to 0.5 and 0.06 with 0.5 M NaCl, obtaining four amaranth isolates named AI pH2-highIS, AI pH8-highIS, AI pH2-lowIS and AI pH8-lowIS [9].…”

Section: Preparation Of Amaranth Isolatesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Amaranth proteins foaming properties: Film rheology and foam stability – Part 2

Bolontrade

Scilingo

Añón

2016

Colloids and Surfaces B: Biointerfaces

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“…Protein solubility and emulsion properties of meat products are closely related (Schut, 1976;Barać et al, 2015). However, protein solubility is closely related to extrinsic factors, such as pH, ionic strength, and temperature (Söderberg, 2013;Bolontrade et al, 2013). Water holding, and oil absorption capacities of pea products increase relative to the protein content of the flour, the protein fraction, and isolate (Sosulski & McCurdy, 1987).…”

Section: Introductionmentioning

confidence: 99%

Model system evaluation of the effects of pea and pH on the emulsion properties of beef

Kurt¹,

Ceylan²

2018

SA J. An. Sci.

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The effects of dried ground pea (0 -1%) and pH (4.80 -7.20) on the emulsion properties of beef were investigated using the model system. The study was designed according to the central composite rotatable design using the Response Surface Methodology. Pea had significant effects on emulsion activity and stability. The effects of pH on emulsion capacity, stability, activity, density, viscosity and apparent yield stress were significant. In addition, the interaction of both factors (pea and pH) caused significant effects on emulsion density, apparent yield stress of emulsion and emulsion gel. Pea addition increased emulsion activity at low concentrations and decreased at high concentrations. This study suggests that pea can improve the properties of emulsion type meat products and may be considered as an alternative additive in such products.

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“…On this account, vegetable proteins are emerging as a promising alternative to partially take the place of animal proteins for human protein (Bolontrade & Scilingo 2013). Soy protein, with nutritionally balanced amino acids, is an important and relatively cheap source of vegetable proteins, so it has been widely used to formulate foods aiming to improve their nutritional and/or functional qualities (Yuan et al 2013;Kim & Kim 2015).…”

mentioning

confidence: 99%

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

Pan¹,

Meng²,

Jiang³

et al. 2017

Czech J. Food Sci.

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Pan M., Meng X., Jiang L., Yu D., Liu T. (2017): Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate. Czech J. Food Sci., 35: 57-66.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.

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Amaranth proteins foaming properties: Adsorption kinetics and foam formation—Part 1

Cited by 37 publications

References 26 publications

Amaranth proteins foaming properties: Film rheology and foam stability – Part 2

Amaranth proteins foaming properties: Film rheology and foam stability – Part 2

Model system evaluation of the effects of pea and pH on the emulsion properties of beef

Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate

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