Impact of processing on functional properties of protein products from wrinkled peas

Fuhrmeister, H.; Meuser, F.

doi:10.1016/s0260-8774(02)00241-8

Cited by 97 publications

(98 citation statements)

References 10 publications

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“…The lowest mean values of EAI were registered at pH 5.0 near isoelectric point of soy and pea proteins, whereas emulsifying activity significantly increased below and above this value. This indicated that solubility was one of the major factors that influenced their emulsifying activity, and was in agreement with previous reports of Fuhrmeister and Meuser (2003), Pesic et al (2005) and Barac et al (2010), which showed a positive relationship between protein solubility and emulsifying activity of pea and soybean protein products. On the other hand, adzuki isolate deviated from this trend.…”

Section: Emulsifying Propertiessupporting

confidence: 93%

“…Furthermore, significantly different functionalities among isolates prepared from the same plant species were observed. Several studies (Pesic et al 2005;Khatib et al 2002;Maninder et al 2007;Barac et al 2010Barac et al , 2011) attributed this to different ratio for the major proteins, which is in turn influenced by genotype characteristics, environmental conditions and processing conditions (Periago et al 1998;Fuhrmeister and Meuser 2003;Dua et al 2009;Taherian et al 2011).…”

Section: Introductionmentioning

confidence: 99%

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Comparative study of the functional properties of three legume seed isolates: adzuki, pea and soy bean

et al. 2014

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The aim of this work was to compare functional properties including solubility, emulsifying and foaming properties of native and thermally treated adzuki, soy and pea protein isolates prepared under the same conditions. These functional properties were tested at four pH values: pH 3.0, pH 5.0, pH 7.0 and pH 8.0. The lowest solubility at all pH values were obtained for isolate of adzuki whereas isolates of soybean had the highest values at almost all pHs. Thermal treatment reduced solubility of soy and pea isolates at all pH values, whereas solubility of adzuki isolate was unchanged, except at pH 8. Native isolate of adzuki had the best emulsifying properties at pH 7.0 whereas at the other pH values some of native pea and soybean protein isolates were superior. After thermal treatment, depending on tested pH and selected variety all of three species could be a good emulsifier. Native soy protein isolates formed the most stable foams at all pHs. Thermal treatment significantly improved foaming properties of adzuki isolate, whereas reduced foaming capacity of soy and pea isolates, but could improve foam stability of these isolates at specific pH. Appropriate selection of legume seed as well as variety could have great importance in achievement of desirable functional properties of final products. All three tested species could find specific application in wide range of food products.

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Section: Emulsifying Propertiessupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Comparative study of the functional properties of three legume seed isolates: adzuki, pea and soy bean

et al. 2014

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“…FC was then measured as the increased (initial) volume of each sample and calculated as follows (Equation 2) according to the method of Fuhrmeister and Meuser (2003):…”

Section: Foam Formation and Measurementmentioning

confidence: 99%

“…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%

“…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). In contrast, PPI prepared by membrane ultrafiltration had better emulsifying and foaming properties than the one prepared by acid or heat precipitation (Fuhrmeister & Meuser, 2003). With regard to pea protein fractions, it was reported that whole albumin isolate had better foaming properties than the lowmolecular weight (MW) fractions (Lu, Quillien, & Popineau, 2000).…”

Section: Introductionmentioning

confidence: 99%

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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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Food Function and Health Benefits of Functional Foods

Panghal¹,

Kumar²,

Kumar³

et al. 2022

Functional Foods

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Impact of processing on functional properties of protein products from wrinkled peas

Cited by 97 publications

References 10 publications

Comparative study of the functional properties of three legume seed isolates: adzuki, pea and soy bean

Comparative study of the functional properties of three legume seed isolates: adzuki, pea and soy bean

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

Food Function and Health Benefits of Functional Foods

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