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Cited by 83

The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.

Mixing plant-based proteins: Gel properties of hemp, pea, lentil proteins and their binary mixtures

Guidi, Sarah, Formica, Florian A., Denkel, Christoph·2022·Food Research International
DOI 10.1016/j.foodres.2022.111752
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Abstract

One of the challenges in substituting dairy products by alternative proteins is that the properties of mixed protein gels cannot necessarily be predicted by those of single protein gels, whereas the need of mixing is often driven by nutritional aspects. However, mixing plant proteins could also open a door to new textures. The main goal of this study was to investigate the impact of binary mixing of hemp (H), yellow pea (P), and brown lentil (L) protein concentrates/isolates on their gel and water-holding properties. Dispersions of reconstituted proteins and mixtures thereof were gelled using glucono-δ-lactone (GDL), transglutaminase (TG), and temperature (T) at a protein content of 12% (w/w). Mixtures of pea and lentil proteins showed gel strengths for TG- and T-induced gels that are proportional to the ratio of the mixture constituents (linear mixing behavior), whereas synergistic effects were observed for GDL-induced gelation. In contrast, all mixtures containing hemp exhibited a non-linear mixing behavior for the three gelation methods, usually resulting in lower gel strengths compared to theoretically expected values. The study showed that mixing plant-based proteins of different protein sources can lead to very different mixing behaviors in terms of gel properties, showing either a reinforcing, an indifferent or a weakening effect compared to the theoretically expected properties. The results can help developing more targeted plant protein-based soft gel products such as yogurt alternatives with specific techno-functional properties, while adjusting the nutritional characteristics.

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Crossref · 10.1016/j.foodres.2022.111752

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Figures

Image 1
CC-BY · From the PDF
Fig. 1 Representation of the experimental workflow performed in this study. Protein extraction from dried material (pea, lentil) and from hemp meal by alkaline solubilization followed by isoelectric precipitation. Preparation of 12% (w/w) protein mixtures, acid-, enzyme- and heat-induced gelation. Gel char­ acterisation by color, gel electrophoresis, texture analysis and water hold­ ing capacity.
Fig. 1 Representation of the experimental workflow performed in this study. Protein extraction from dried material (pea, lentil) and from hemp meal by alkaline solubilization followed by isoelectric precipitation. Preparation of 12% (w/w) protein mixtures, acid-, enzyme- and heat-induced gelation. Gel char­ acterisation by color, gel electrophoresis, texture analysis and water hold­ ing capacity.CC-BY · From the PDF
Fig. 2 Protein extraction yield (solid bars, left Y-axis) and protein content (dashed bars, right Y-axis) in the freeze-dried protein concentrates/isolates. Although the extraction procedure was performed three times, the protein content was only quantified once. The standard conversion of 6.25 was used for calculation.
Fig. 2 Protein extraction yield (solid bars, left Y-axis) and protein content (dashed bars, right Y-axis) in the freeze-dried protein concentrates/isolates. Although the extraction procedure was performed three times, the protein content was only quantified once. The standard conversion of 6.25 was used for calculation.CC-BY · From the PDF
Image 4
CC-BY · From the PDF
Fig. 4 Visual representation and whiteness index of the different gels. Each single protein source is represented on an axis, separated by a 120 ◦ angle, the protein mixtures can be found in between, each separated by a 30 ◦ angle. Each symbol color represents the color of the gel converted to RGB values (using a L*a*b* to RGB converter) and the distance from the center represents the whiteness index (WI, calculated with equation (2), the higher the index, the whiter the sample). The three gelation methods, glucono-delta-lactone (GDL), transglutaminase (TG) and temperature (T) are represented with three different colors, black, red and blue for the connecting lines, respectively. Dot-dashed lines represent the expected WI values. Around the graph: photographs of the different gel mixtures and ratios for each type of gel. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
Fig. 4 Visual representation and whiteness index of the different gels. Each single protein source is represented on an axis, separated by a 120 ◦ angle, the protein mixtures can be found in between, each separated by a 30 ◦ angle. Each symbol color represents the color of the gel converted to RGB values (using a L*a*b* to RGB converter) and the distance from the center represents the whiteness index (WI, calculated with equation (2), the higher the index, the whiter the sample). The three gelation methods, glucono-delta-lactone (GDL), transglutaminase (TG) and temperature (T) are represented with three different colors, black, red and blue for the connecting lines, respectively. Dot-dashed lines represent the expected WI values. Around the graph: photographs of the different gel mixtures and ratios for each type of gel. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)CC-BY · From the PDF
Fig. 5 Gel strengths of the single and binary gels. a) Average load during penetration test at plateau (i.e. the last 1.5 mm) as a function of the ratio, the mixtures, and the gel type. The curves are the average of triplicate measure­ ments for each process, which was itself repeated two times (n = 6). The symbols represent the average while standard deviation is shown using shadows. b) Ratios between the measured value and theoretical value (assuming that the gel strength of a protein mixture is proportional to the gel strengths of the proteins composing it, meaning values < 1 represent a dilution effect or antagonistic, destructive interactions and values > 1 represent syn­ ergistic, constructive interactions). Statistical differences to a linear mixing behavior (ratio = 1.0) are indicated (* p < 0.05, ** p < 0.01, *** p < 0.001).
Fig. 5 Gel strengths of the single and binary gels. a) Average load during penetration test at plateau (i.e. the last 1.5 mm) as a function of the ratio, the mixtures, and the gel type. The curves are the average of triplicate measure­ ments for each process, which was itself repeated two times (n = 6). The symbols represent the average while standard deviation is shown using shadows. b) Ratios between the measured value and theoretical value (assuming that the gel strength of a protein mixture is proportional to the gel strengths of the proteins composing it, meaning values < 1 represent a dilution effect or antagonistic, destructive interactions and values > 1 represent syn­ ergistic, constructive interactions). Statistical differences to a linear mixing behavior (ratio = 1.0) are indicated (* p < 0.05, ** p < 0.01, *** p < 0.001).CC-BY · From the PDF
Fig. 6 Water holding capacity of the different gels. a) average of the water holding capacity depending on the ratio, the mixture and the gel type. The curves are the average of six measurements coming from two hydration pro­ cesses (the symbols representing the average and the shaded areas, the standard deviation; n = 6). b) ratios between the measured value and theoretical value (assuming that the gel strength of a protein mixture is proportional to the gel strengths of the proteins composing it, meaning values < 1 represent a dilution effect or antagonistic, destructive interactions and values > 1 represent syn­ ergistic, constructive interactions). Statistical differences to a linear mixing behavior (ratio = 1.0) are indicated (* p < 0.05, ** p < 0.01, *** p < 0.001).
Fig. 6 Water holding capacity of the different gels. a) average of the water holding capacity depending on the ratio, the mixture and the gel type. The curves are the average of six measurements coming from two hydration pro­ cesses (the symbols representing the average and the shaded areas, the standard deviation; n = 6). b) ratios between the measured value and theoretical value (assuming that the gel strength of a protein mixture is proportional to the gel strengths of the proteins composing it, meaning values < 1 represent a dilution effect or antagonistic, destructive interactions and values > 1 represent syn­ ergistic, constructive interactions). Statistical differences to a linear mixing behavior (ratio = 1.0) are indicated (* p < 0.05, ** p < 0.01, *** p < 0.001).CC-BY · From the PDF

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Research works printed but not linked: 1

  1. Liu, 2022, Composition and Functional Properties of Hemp Seed Protein Isolates from Various Hemp Cultivars (preprint), Biochemistry

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Metadata

Authors
Guidi, S., Formica, F. A., & Denkel, C.
Venue
Food Research International
Publisher
Elsevier BV
Published
2022-11
Volume
161
Pages
111752
ISSN
0963-9969
DOI
10.1016/j.foodres.2022.111752
Cited by
83
References
53
Language
en
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