pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins

Liang, Han-Ni; Tang, Chuan-He

doi:10.1016/j.foodhyd.2013.04.005

Cited by 303 publications

(177 citation statements)

References 44 publications

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“…The stability exhibited by the emulsions at pH 9.0 may be due to the high solubility and abundance of charged protein molecules, which were able to enhance repulsions between oil droplets and reduce the rate of coalescence. An opposite effect of pH and droplet size on stability of emulsions was reported for pea proteins when compared to those obtained for CPI and CPH in this study, with pea proteins exhibiting better emulsifying abilities at pH 3.0 when compared to pH 9.0 (Liang & Tang, ).…”

Section: Resultscontrasting

confidence: 72%

“…This is because proteins are generally least soluble around their isoelectric point as the net charge is negligible at this point, and there is a formation of aggregates because of hydrophobic interactions (Sorgentini & Wagner, ). The improvement in solubility at pH 4.0 has also been reported for several modified plant proteins (Vioque et al ., ; Sorgentini & Wagner, ; Kong et al ., ; Liang & Tang, ).…”

Section: Resultsmentioning

confidence: 99%

“…This further buttresses the effect of protein aggregation around its isoelectric point and the ability of enzyme hydrolysis to unfold the protein structure with peptide cleavage over time. This shows that besides solubility, other parameters such as the surface hydrophobicity/charge, protein–protein interactions and conformational flexibility of the proteins at the oil–water interface can contribute to the emulsion‐forming capacity and/or emulsion stability of proteins when used as emulsifiers (Liang & Tang, ). TH‐formed emulsions were found to be the most stable, which indicates the presence of highly charged peptide molecules.…”

Section: Resultsmentioning

confidence: 99%

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Influence of enzymatic hydrolysis, pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

Alashi

Blanchard

Mailer

et al. 2018

Int J of Food Sci Tech

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Summary The aim of this work was to enhance emulsification properties of canola proteins through enzymatic proteolysis and pH variaton. Canola protein isolate (CPI) and hydrolysates (CPHs) were used to form emulsions at pH 4.0, 7.0 and 9.0 followed by storage at 4 or 25 °C for 7 days. Controlled enzymatic hydrolysis led to increased peptide bond cleavage with time (0.23 g/100 g in CPI to 7.18 g/100 g after 24‐h Alcalase hydrolysis). Generally, oil droplet sizes were smaller for emulsions made at pH 9.0, which suggest better quality than those made at pH 4.0 and 7.0. Trypsin hydrolysate emulsions were the most physically stable at pH 7.0 and 9.0; in contrast, the pepsin hydrolysate emulsions were unstable at all conditions. The results suggest that selective enzymatic hydrolysis could play an important role in enhancing successful incorporation of canola proteins and peptides into food systems as protein emulsifiers.

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Section: Resultscontrasting

confidence: 72%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Influence of enzymatic hydrolysis, pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

Alashi

Blanchard

Mailer

et al. 2018

Int J of Food Sci Tech

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“…For example, oil droplet size of emulsions formed with PPI was reduced when alkalinity of the aqueous phase increased from pH 4.0 to 9.0; in contrast, foam volume and foam stability (FS) were increased (Adebiyi & Aluko, 2011). PPI was also reported to have better emulsifying activity (smaller oil droplet size) at pH 3.0 and 7.0 when compared to pH 5.0 (Chang, Tu, Ghosh, & Nickerson, 2015;Liang & Tang, 2013). With respect to protein isolation method, the PPI produced by isoelectric protein precipitation formed smaller emulsion oil droplets than the saltextracted PPI (Karaca, Low, & Nickerson, 2011).…”

Section: Introductionmentioning

confidence: 99%

Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment

Chao

Aluko

2018

CyTA - Journal of Food

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Pea protein isolate (PPI) prepared through isoelectric protein precipitation was heat-treated between 50°C and 100°C. The effect of heat treatment on the structural and functional properties of proteins was evaluated. Native gel electrophoresis showed the formation of protein aggregates (molecular weight ≫ 200 kDa) in the temperature range of 80-100°C. Intrinsic fluorescence data suggested that protein denaturation reached its highest level at pH 3.0. The formation of oil-inwater emulsions (1:5 oil:water volume ratio) was positively impacted by pH increase as evidenced by the decrease of minimum oil droplet size (d 4,3 ) from 26 μm at pH 5.0 to 22 μm at pH 7.0 (P < 0.05). In contrast, heat pretreatment led to decreasing emulsion properties at pH 3.0 with d 4,3 values increasing from 27 μm to 80 μm (P < 0.05). Regardless of pH applied, all heated PPI samples displayed low foaming properties.Modificación mediante pretratamiento térmico de las propiedades estructurales, emulsificantes y espumantes de una proteína de arveja [guisante] aislada RESUMEN El aislado de proteína de arveja (PPI), preparado mediante precipitación isoeléctrica de proteínas, se sometió a un tratamiento térmico con temperaturas de entre 50 y 100°C. Posteriormente, se evaluó el efecto del tratamiento térmico en las propiedades estructurales y funcionales de las proteínas. La electroforesis nativa en gel reveló la formación de agregados proteicos (peso molecular ≫ 200 kDa) en el rango de temperatura de 80 a 100°C. Los datos obtenidos de la fluorescencia intrínseca sugieren que la desnaturalización de las proteínas alcanzó su nivel más elevado cuando el pH era 3.0. La formación de emulsiones de aceite en agua (ratio del volumen aceite:agua 1:5) se vio afectada positivamente por el aumento del pH, lo que se evidenció por la disminución del tamaño mínimo de la gota de aceite (d 4,3 ), que pasó de 26 μm con pH de 5.0 a 22 μm con pH de 7.0 (P < 0.05). En contraste, el pretratamiento térmico produjo una disminución de las propiedades de emulsión cuando el pH era 3.0, pues los valores d 4,3 aumentaron de 27 μm a 80 μm (P < 0.05). Independientemente del pH utilizado, todas las muestras de PPI calentadas presentaron limitadas propiedades espumantes. ARTICLE HISTORY

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“…SPI has many functional properties of emulsifying, foaming, gelation and film forming [4] . Moreover, SPI is also abundant in nutrients and has the features of reducing serum cholesterol and preventing cardiopathy and cerebrovascular disease.…”

Section: Introductionmentioning

confidence: 99%

Effects of xanthan gum on the rheological properties of soy protein dispersion

Bi¹,

Gao²,

Zhu³

et al. 2018

International Journal of Agricultural and Biological Engineering

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This study focused on the effects of addition of xanthan gum (XG) on the rheological properties of soy protein isolate (SPI) solution. Three types of tests (steady shear test, strain sweep test, and frequency sweep test) were performed to figure out the influences of shear rate on the viscosity of the SPI-XG hybrid system, the effects of strain variable on the storage modulus of the hybrid system, and the effects of frequency on both the storage modulus and the loss modulus of the hybrid system, respectively. SPI-XG hybrid system showed more obvious shear-thinning properties compared to pure SPI and pure XG solution. Meanwhile, it was found that the critical point of hybrid system was highly related to the XG concentration. XG can postpone the critical point strain amplitude to a higher value, and the addition of XG can enhance the strain resistance of hybrid system. The concentration of XG influenced the viscoelastic frequency dependence of the hybrid system significantly and complicatedly. After the addition of XG, the correlation between G′ and frequency changed from negative to positive.

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pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins

Cited by 303 publications

References 44 publications

Influence of enzymatic hydrolysis, pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

Influence of enzymatic hydrolysis, pH and storage temperature on the emulsifying properties of canola protein isolate and hydrolysates

Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment

Effects of xanthan gum on the rheological properties of soy protein dispersion

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