CO2-defatted oats: Solubility, emulsification and foaming properties

Konak, Ülgen İlknur; Ercili-Cura, Dilek; Sibakov, Juhani; Sontag‐Strohm, Tuula; Certel, Muharrem; Loponen, Jussi

doi:10.1016/j.jcs.2014.01.013

Cited by 49 publications

(47 citation statements)

References 25 publications

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“…The increase in protein solubility found in oat protein concentrate (OPI in Table 2) at neutral and especially alkaline pH was also reported by Nivala, Mäkinen, Kruus, Nordlund, & Ercili-Cura [31], Konak et al [3], Ma and Harwalkar [4], Loponen et al [32] and Guan et al [5]. The increase in solubility at alkaline pH was attributed to an increase in protein net charge.…”

Section: Molecular Characteristics and Protein Solubilitysupporting

confidence: 73%

“…emulsification [1] and foaming [2][3][4] properties have previously been investigated. However, molecular characteristics such as high molecular weight protein profile and low solubility in acidic pH limit its use as functional ingredient in dispersed food systems such as foams and emulsions [3,5]. Physical, chemical or enzymatic treatments have demonstrated the potential to modify the structure of oat protein improving solubility, emulsion and/or foaming properties [6].…”

Section: Introductionmentioning

confidence: 99%

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Foaming characteristics of oat protein and modification by partial hydrolysis

Brückner-Gühmann

Heiden-Hecht

Sözer

et al. 2018

Eur Food Res Technol

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Foaming ability of oat protein isolate (OPI) was analysed at pH 4 and 7. Foaming properties were influenced by partial hydrolysis with trypsin (OPT) and alcalase (OPA). The viscoelasticity of the protein film, the interactions between the protein molecules, and the network forming within the protein film were analysed by interfacial rheology. At pH 7, foams made of OPI and OPT were found to be stable with OPI having the fastest foaming ability. At pH 4, the foaming properties of OPI were found to be poor due to limited solubility. The specific cleavage behaviour of trypsin improved the foaming properties, especially at pH 4, resulting in a homogenous foam structure, a fast foaming ability and a highly viscoelastic interfacial film. The formation of a thick steric protein layer at pH 7 and the formation of strong hydrophobic interactions at pH 4 were found to be the dominating foam stabilisation mechanisms. In conclusion, oat protein ingredients were developed with targeted functional properties.

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Section: Molecular Characteristics and Protein Solubilitysupporting

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Foaming characteristics of oat protein and modification by partial hydrolysis

Brückner-Gühmann

Heiden-Hecht

Sözer

et al. 2018

Eur Food Res Technol

View full text Add to dashboard Cite

show abstract

“…This would favor the aggregation of protein molecules because there would be fewer repulsive forces and hence a low protein solubility. The maximum solubility of proteins obtained from WF was observed at pH 10.5 (Konak et al, ) due to the increased net charge of proteins and availability of attractive forces with water. In other works, the solubility of oat proteins has increased in highly acidic conditions (pH 1–4) (Ma & Harwalkar, ; Nieto‐Nieto et al, ); however, the present study did not consider beyond pH 3, which is not typically used in food products.…”

Section: Resultsmentioning

confidence: 99%

Structural Characterization and Functional Properties of Proteins from Oat Milling Fractions

Walters

Udenigwe

Tsopmo

2018

J Americ Oil Chem Soc

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The aim of this work was to study the structure and functionalities of proteins from commercial oat milling fractions. Protein isolates obtained from fine (FB), medium (MB), and low (LB) oat brans, and whole oat groat flour (WF) contained 75.0-97.1% proteins. However, the protein content of the products of 15% (15% high glucan [15HG]) and 20% (20% high glucan [20HG]) HG flours were four fold less because of their high carbohydrate contents (~75%). There was no apparent difference in molecular weights of the polypeptides (20, 35, 60, and 150 kDa) contained in these protein products. Protein profiling using mass spectrometry showed that avenin was not detected in FB and MB because of their relatively high concentrations of 11-12S globulins. Secondary structural features of the molecules and microstructure details of the gelled proteins were similar for proteins from FB, MB, LB, and WF, but different from those of 15HG and 20HG. Similarly, these differences in the structural features of proteins of the milling fractions were reflected in their water-holding capacity and the solubility properties of the protein products.

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“…The total soluble matter depends on multiple factors, including the origin of the species, chemical composition and processing parameters in terms of the method for removing the fat, time of heating, temperature, pH, the ionic strength of the aqueous solvent, the speed of blending as well as the Table 2 Amino acid composition of control soy flour (CSF), defatted soy flour by SC-CO 2 (DSFSC-CO 2 ), and defatted soy flour by organic solvent (DSF-OS) (Unit: g/100 g) degree of agitation. It was demonstrated by Konak et al (2014) that the solubility of CO 2 -oat protein was significantly higher under alkaline conditions than acidic conditions because of the increase in net protein charge. The current study was conducted at neutral pH and it was found that DSFSC-CO 2 had a significantly greater (p \ 0.05) TSS content (69.77%) than DSF-OS (65.65%) and CSF (64.39%), as shown in Fig.…”

Section: Total Soluble Solids Contentsmentioning

confidence: 99%

Comparative study of the quality characteristics of defatted soy flour treated by supercritical carbon dioxide and organic solvent

et al. 2017

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Defatted soy flour is a potential source of food protein, amino acids, ash and isoflavones. The supercritical carbon dioxide (SC-CO) and a traditional organic solvent extraction methods were used to remove fat from soy flour, and the quality characteristics of a control soy flour (CSF), defatted soy flour by SC-CO (DSFSC-CO) and defatted soy flour by an organic solvent (DSF-OS) were compared. The SC-CO process was carried out at a constant temperature of 45 °C, and a pressure of 40 MPa for 3 h with a CO flow rate of 30 g/min. The DSFSC-CO had significantly higher protein, ash, and amino acids content than CSF and DSF-OS. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis demonstrated that CSF and DSFSC-CO had protein bands of similar intensity and area that indicated no denaturation of protein, whereas DSF-OS showed diffuse bands or no bands due to protein denaturation. In addition to higher nutritional value and protein contents, DSFSC-CO showed superior functional properties in terms of total soluble solids content, water and oil absorption, emulsifying and foaming capacity. The SC-CO method offers a nutritionally and environmentally friendly alternative extraction processing approach for the removal of oil from high-protein food sources. It has a great potential for producing high-protein fat-free, and low-calorie content diet than the traditional organic solvent extraction method.

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CO2-defatted oats: Solubility, emulsification and foaming properties

Cited by 49 publications

References 25 publications

Foaming characteristics of oat protein and modification by partial hydrolysis

Foaming characteristics of oat protein and modification by partial hydrolysis

Structural Characterization and Functional Properties of Proteins from Oat Milling Fractions

Comparative study of the quality characteristics of defatted soy flour treated by supercritical carbon dioxide and organic solvent

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