“Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”

López, Débora Natalia; Ingrassia, Romina; Busti, Pablo; Bonino, Julia; Delgado, Juan Francisco; Wagner, Jorge R.; Boeris, Valeria; Spelzini, Darío

doi:10.1016/j.lwt.2017.12.060

Cited by 30 publications

(25 citation statements)

References 34 publications

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“…). This fact could be associated with an aggregation process of the previously denatured proteins caused by the release of energy in a structure formation with an associated enthalpy of 17.6 ± 0.7 J g −1 (dry basis) …”

Section: Resultsmentioning

confidence: 99%

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Emulsifying properties of defatted rice bran concentrates enriched in fiber and proteins

et al. 2019

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BACKGROUND: Rice bran (RB), a by-product of the rice milling industry, constitutes around 10% of the total weight of rough rice. The interest in the use of RB is centered on its nutritional quality, its low cost, and its extensive worldwide production. As RB is commonly used for oil extraction, the defatted rice bran (DRB) is obtained as a second by-product. The aim of this work was to obtain a defatted rice bran concentrate (DRBC), enriched in protein and fiber, from defatted rice bran flour (DRBF) and to determine its physicochemical and emulsifying properties. RESULTS: To obtain the DRBC, the starch was efficiently hydrolyzed (> 98%) with -amylase and amyloglucosidase, with a concomitant increase in the proportions of crude protein (from 154.7 to 274.3 g kg −1 ) and total dietary fiber (from 276.1 to 492.3 g kg −1 ). Defatted rice bran concentrate exhibited a loss of protein solubility and increased surface hydrophobicity compared with DRBF. Defatted rice-bran concentrate dispersions with and without previous ultrasound treatment were prepared. The sonication led to an increase in the apparent viscosity. Emulsions were prepared with dispersions with and without previous ultrasound treatment and showed high stability in quiescent conditions over 28 days. However, the emulsions prepared with dispersions treated with ultrasound resulted in lower D 4,3 values and higher elastic and viscous moduli. CONCLUSION: The rice bran concentrate can be used to obtain stable oil-in-water (O/W) emulsions, including both soluble andinsoluble fractions, in acidic and neutral conditions. These innovative findings thus contribute to increasing the added value of this important by-product of the rice-milling industry. Surface hydrophobicity (H 0 )Aromatic surface hydrophobicity was determined on a soluble protein fraction of samples prepared as detailed above, following the approach described by Fernández-Fernández et al., 31 based on J Sci Food Agric 2020; 100: 1336-1343

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Section: Resultsmentioning

confidence: 99%

“…An empty aluminum pan was used as reference. The thermograms were obtained at a heating rate of 5 °C min −1 in the range of 10–130 °C . The Tp and Δ H were obtained from the analysis of thermograms with Universal Analysis 2000 software (TA Instruments, LLC Waters).…”

Section: Methodsmentioning

confidence: 99%

Emulsifying properties of defatted rice bran concentrates enriched in fiber and proteins

et al. 2019

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“…Chia protein isolates (CPI) were obtained through isoelectric precipitation. Two different conditions were assayed with the aim of studying the effect of extraction pH on the surface properties [5]. Milled and partially defatted chia seeds were hydrated with distilled water (1:20) and stirred for 30 min.…”

Section: Preparation Of Chia Protein Isolatesmentioning

confidence: 99%

“…The effect of the extraction conditions on the structural properties of chia protein isolates (CPI) has recently been demonstrated [5]. These isolates showed desirable functional properties for use in the food industry [6].…”

Section: Introductionmentioning

confidence: 99%

Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization

López

Boeris

Spelzini

et al. 2019

Colloids and Surfaces B: Biointerfaces

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Highlights  Chia proteins were isolated from defatted milled seeds at pH 10 (CPI10) or 12 (CPI12)  The interfacial behavior of these isolates was related to their extraction conditions  Foams from CPI10 were more stable due to the formation of a thicker interfacial film  CPI10 showed a greater ability to retard liquid drainage  CPI12 showed better emulsifying properties whereas poorer foaming properties

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“…For the three analyzed samples, the absolute values of zeta potential increased as the pH increased, being higher at pH 10 (−40.10–44.40 mV) > pH 7 (−31.50–35.50 mV) > pH 4 (−18.50–19.90 mV). These values demonstrate that at pH 10, the isolates show more negative zeta potential values indicating a greater repulsion between the protein particles and a greater electrostatic stabilization (López et al, ) that helps to explain the highest values of solubility, foaming, and emulsifying capacity. Particle size decreased with the increasing pH being significantly lower ( p < .05) at pH 10 for QPI (230.20 nm) and QPI‐FL (240.50 nm).…”

Section: Resultsmentioning

confidence: 95%

Influence of heat denaturation and freezing–lyophilization on physicochemical and functional properties of quinoa protein isolate

et al. 2020

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Backgrounds and objectives Quinoa protein isolate has been shown to confer significant health benefits. However, it is necessary to evaluate the effect of processing on its properties. Therefore, the aim of this work was to evaluate the influence of heat denaturation or freezing followed by lyophilization on the physicochemical and functional properties of the quinoa protein isolate. Findings Freezing–lyophilization of quinoa protein isolate (QPI‐FL) exhibited a higher foaming capacity and emulsifying capacity at pH 10, and the oil retention capacity was ten times greater that exhibited by the unmodified quinoa protein isolate (QPI), while the particle size and water and oil retention capacity in the modified protein isolate by heat denaturation (QPI‐HD) were twice as compared to QPI. The pH had a significant effect on all physicochemical and functional properties. The flow properties and the micrograph analysis of modified protein isolates revealed greater porosity in comparison with those of the unmodified protein isolate. QPI‐FL showed higher water adsorption capacity at high water activity and a greater displacement in the thermal transitions. Conclusions In general, heating did not significantly affect the functional properties of the quinoa protein isolate, while the freezing–lyophilization improved them, which may be of interest in the processes of foods that include in their process the heating or freezing. Significance and novelty Quinoa protein isolate can be added to different food products with the purpose of improving its composition. However, heating and freezing are two frequent operations in most processes that could affect their properties.

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“Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds”

Cited by 30 publications

References 34 publications

Emulsifying properties of defatted rice bran concentrates enriched in fiber and proteins

Emulsifying properties of defatted rice bran concentrates enriched in fiber and proteins

Adsorption of chia proteins at interfaces: Kinetics of foam and emulsion formation and destabilization

Influence of heat denaturation and freezing–lyophilization on physicochemical and functional properties of quinoa protein isolate

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