Influence of pH and ionic strength on the thermal gelation behaviour of pea protein

Tanger, Caren; Müller, M.G.; Andlinger, David J.; Kulozik, Ulrich

doi:10.1016/j.foodhyd.2021.106903

Cited by 80 publications

(32 citation statements)

References 45 publications

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“…This indicates that at pH 5 and 7, protein−protein interaction is promoted and is accompanied by a decrease of protein−water association, resulting in a compact microstructure with a low water content and leading to high values of the G′ and G″ of the gels obtained at pH 5 and 400 and 600 MPa HHP treatments. In the case of heat treatment, the gels induced at pH 5 are also stiffer than those obtained at pH 7 and 9, which is consistent with the recent work by Tanger et al (2021) who found that pea protein isolate gelation at 95 °C resulted in a much stiffer gel at pH 4.5 than at pH 7 and 9. 35 For a large deformation rheology, G′ and G″ as a function of applied strain is illustrated in Figure 4B,D,F.…”

Section: Methodssupporting

confidence: 90%

“…In the case of heat treatment, the gels induced at pH 5 are also stiffer than those obtained at pH 7 and 9, which is consistent with the recent work by Tanger et al (2021) who found that pea protein isolate gelation at 95 °C resulted in a much stiffer gel at pH 4.5 than at pH 7 and 9. 35 For a large deformation rheology, G′ and G″ as a function of applied strain is illustrated in Figure 4B,D,F. All samples exhibit qualitatively similar behavior, and G′ and G″ are independent of the applied strain until reaching a critical strain value, which is defined as the LVR region.…”

Section: Methodssupporting

confidence: 90%

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Impact of High Hydrostatic Pressure on the Gelation Behavior and Microstructure of Quinoa Protein Isolate Dispersions

Lan

Zhang

Palmer

et al. 2021

ACS Food Sci. Technol.

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The gelation of 10 w/w % quinoa protein isolate (QPI) dispersions induced by high hydrostatic pressure (HHP) at three pHs (5, 7, and 9) was investigated. HHP was conducted at 20 °C for 15 min at 100, 250, 400, and 600 MPa. Thermally induced gelation (81 ± 2 °C, 30 min) was also conducted as a comparison to HHP. Both thermal and HHP (above 250 MPa) treatments can induce protein gelation, and the viscosity and elasticity of the gels increased with the increase in pressure levels. The gels formed either by heat or HHP treatment at pH 5 exhibit a stronger gel strength and a compact network structure than at pH 7 and 9. Confocal microscopy showed that HHP treatment formed a heterogenous and well-spanned network with large protein aggregates, while heat treatment resulted in a more homogeneous structure. SDS−PAGE revealed that QPI gels were formed by the denaturation and aggregation of 11S globulin.

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Section: Methodssupporting

confidence: 90%

Section: Methodssupporting

confidence: 90%

Impact of High Hydrostatic Pressure on the Gelation Behavior and Microstructure of Quinoa Protein Isolate Dispersions

Lan

Zhang

Palmer

et al. 2021

ACS Food Sci. Technol.

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“…The viscoelastic properties of PPI/WPI solutions were investigated by oscillatory measurements, as described elsewhere . For this, a Paar Physica MCR 302 (Anton Paar GmbH, Graz, Austria) stress-controlled rheometer with a concentric cylinder geometry CC10 (bob diameter 9.995 mm, cup diameter 10.842 mm) was used.…”

Section: Methodsmentioning

confidence: 99%

“…The viscoelastic properties of PPI/WPI solutions were investigated by oscillatory measurements, as described elsewhere. 28 For this, a Paar Physica MCR 302 (Anton Paar GmbH, Graz, Austria) stresscontrolled rheometer with a concentric cylinder geometry CC10 (bob diameter 9.995 mm, cup diameter 10.842 mm) was used. The temperature of the rheometer was controlled with a Peltier element cooled by an accompanying recirculating cooler model Haake DC1 (Thermo Haake GmbH, Karlsruhe, Germany).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Viscoelasticity and Protein Interactions of Hybrid Gels Produced from Potato and Whey Protein Isolates

Andlinger

Rampp

Tanger

et al. 2021

ACS Food Sci. Technol.

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Controlling the textural properties of protein gels is of high importance for designing food and other protein products. The combination of animal-derived proteins and plant-based proteins offer the possibility to create nutritional, sustainable, and also textural advantageous products. However, interactions between proteins from different sources and with different molecular features are not well-understood yet. By analyzing the interactions between whey (WPI) and potato proteins (PPIs), we can determine how gel structures in protein gels form. Through different mixing ratios, pH levels, and ionic strengths, we show how the formation of disulfide and hydrophobic bonds influence the textural properties of protein gels. It could be shown that, up to a 50:50 mixing ratio, the properties of PPI dominate those of WPI. Gels with a high elasticity could be formed only through the development of a continuous disulfide network.

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“…The mineral content of the supernatants is composed of native minerals from the pea and sodium from the added NaOH. The mineral content has to be taken into consideration for application of the protein fractions, as an increasing mineral content leads to an increase in denaturation temperature independent from pH, as NaCl stabilizes the quaternary structure of protein [18,26,27]. Due to that, gel formation is hindered and the gel stiffness is reduced.…”

Section: Dry Matter and Protein Contentmentioning

confidence: 99%

Upscaling of alkaline pea protein extraction from dry milled and pre-treated peas from laboratory to pilot scale: Optimization of process parameters for higher protein yields

et al. 2022

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The upscaling of pea protein extraction from laboratory scale with a centrifuge to pilot scale with a decanter centrifuge was investigated, and the pea protein extraction efficiency from dry milled and pre-treated peas was compared. Upscaling from laboratory to pilot scale is possible since starch was under the limit of detection (< 0.5%). The protein banding pattern of a sodium-dodecyl-sulfate polyacrylamide gel electrophoresis confirmed that albumins and globulins were extracted by alkali extraction. Protein yield increased from 59.5% to 67.1% for dry milled peas due to constant and quick discharge of dry matter in the decanter centrifuge. For pre-treated peas, the protein yield increased from 60.3% to 94.3%, which is explained by an improved cutting and improved separation in pilot scale compared to laboratory scale. The impact of acceleration, mass flow, differential speed and their respective interactions in the decanting process was determined with a design of experiments. For dry milled peas, only the mass flow exceeded the significance level. However, a mass flow of 5 kg h−1, an acceleration of 1000 g$$\times$$ × and a differential speed of 50 min−1 led to the highest protein yield of 75.6%. The obtained protein yields for the pre-treated peas were in the range of 83 to 96% and therefore did not show significant differences in protein yield.

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Influence of pH and ionic strength on the thermal gelation behaviour of pea protein

Cited by 80 publications

References 45 publications

Impact of High Hydrostatic Pressure on the Gelation Behavior and Microstructure of Quinoa Protein Isolate Dispersions

Impact of High Hydrostatic Pressure on the Gelation Behavior and Microstructure of Quinoa Protein Isolate Dispersions

Viscoelasticity and Protein Interactions of Hybrid Gels Produced from Potato and Whey Protein Isolates

Upscaling of alkaline pea protein extraction from dry milled and pre-treated peas from laboratory to pilot scale: Optimization of process parameters for higher protein yields

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