Physicochemical and textural properties of heat-induced pea protein isolate gels

Shand, P.J.; Ya, H.; Pietrasik, Z.; Wanasundara, P. K. J. P. D.

doi:10.1016/j.foodchem.2006.06.060

Cited by 335 publications

(245 citation statements)

References 41 publications

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“…3). These peaks in soya correspond to thermal denaturation temperatures of β-conglycinin and glycinin, respectively (Shand, Ya, Pietrasik, & Wanasundara, 2007). The single transition observed in marama occurred at a higher temperature than did soya glycinin (11S) and was very broad.…”

Section: Resultsmentioning

confidence: 93%

Highly viscous dough-forming properties of marama protein

et al. 2012

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Marama bean is an indigenous Southern African oilseed legume with an unusual protein composition. Hence, its rheological properties were studied. Marama protein formed a highly viscous and extensible dough when compared to soya and gluten.With a dough of 38% moisture, marama protein extensibility was very high (304%), twice that of gluten and soya, and this increased considerably (> 3 fold) when the moisture content was increased to 45%. With added peroxidase, the storage modulus (G') of marama protein dough increased with time, suggesting the formation of new and strong protein networks. Dityrosine crosslinks were detected in the doughs.Marama protein showed a single transition with a denaturation temperature higher than soya glycinin. Marama protein appeared more hydrophobic and contained more β-sheet structure than soya. Thus, the highly viscous and extensible rheological behaviour of marama protein is probably related to its high β-sheet conformation, hydrophobic interactions and tyrosine crosslinks.

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Section: Resultsmentioning

confidence: 93%

Highly viscous dough-forming properties of marama protein

et al. 2012

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“…Native pea globulins are salt-soluble proteins; the highest level of protein solubility (PS) is reached above pH 6.0 and below pH 4.0 (Adebiyi & Aluko, 2011). However, in case of an extraction procedure that could alter protein structure (by the use of strong acid/alkali, heating procedure, spray-drying), the level of insoluble protein is increased due to the formation of large aggregates (Fuhrmeister & Meuser, 2003;Shand, Ya, Pietrasik, & Wanasundara, 2007). The first condition to ensure satisfying functional properties is a low-denatured state, which enhances PS at the pH of interest.…”

Section: Introductionmentioning

confidence: 99%

“…Analysis of various pea seed flours has confirmed the superior ability of proteins to form and stabilize oil-in-water emulsions when compared to polysaccharides (Aluko, Mofolasayo, & Watts, 2009). A commercial PPI exhibited gelling abilities, though addition of NaCl was required for increased gel strength (Shand et al, 2007). An important finding was the extensive denaturation of proteins in commercial PPIs when compared to their laboratory-prepared counterparts.…”

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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“…Knowledge of the grain microstructure may be important in the extraction, processing and utilisation of protein (Aguilera 2005;Parada and Aguilera 2007). The physical localisation of protein bodies relative to either the lipids has been found to influence protein extractability (Shand et al 2007) and functional properties such as protein digestibility (Aguilera 2005). Grain microstructure also affects grain hardness (Aguilera and Stanley 1999), an important parameter in milling operations and equipment design for processing.…”

Section: Introductionmentioning

confidence: 99%

Chemical composition and microstructure of Bauhinia grains

2014

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Bauhinia is a leguminous plant species found in almost every part of the world, including southern Africa. In this study, grain composition and protein body microstructure of two indigenous southern African Bauhinia species, B. galpinii and B. petersiana were determined. Protein (38 g/100 g) and fat (23 g/100 g) were the major constituents of Bauhinia. Bauhinia grains also contained substantial amounts of zinc (6 mg/100 g) and iron (3 mg/100 g) when compared to FAO/WHO standards. The parenchyma cells of Bauhinia showed spherical protein bodies with globoids inclusions and these were surrounded by lipids. However, the protein bodies of B. petersiana were smaller in size (7±3 μm) than those of B. galpinii (13±4 μm). The microstructure of protein bodies in Bauhinia is very similar to that of soya, suggesting that the processing technology developed for soya protein may be adopted for Bauhinia.

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Physicochemical and textural properties of heat-induced pea protein isolate gels

Cited by 335 publications

References 41 publications

Highly viscous dough-forming properties of marama protein

Highly viscous dough-forming properties of marama protein

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

Chemical composition and microstructure of Bauhinia grains

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