Functional properties of protein preparations from amaranth seeds in model system

Tömösközi, Sándor; Gyenge, L.; Pelcéder, Á.; Varga, József; Abonyi, Tibor; Lásztity, R.

doi:10.1007/s00217-007-0663-3

Cited by 24 publications

(19 citation statements)

References 11 publications

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“…Amaranth albumins foam better and yield foams with better stability than amaranth proteins extracted under alkaline conditions. The latter, in turn, foam better than amaranth globulins (Tömösközi and others ). The foaming properties of amaranth albumins are even similar to those of casein (Tömösközi and others ) and egg albumins at acidic pH values (Silva‐Sanchez and others ).…”

Section: Techno‐functional Propertiesmentioning

confidence: 93%

“…In general, the solubility of amaranth, buckwheat, and quinoa proteins is poor (range of 2 to 35% range) in a pH ranging from 3.0 to 5.0. Maximum solubility, with percentages ranging from 50 to almost 100%, is found at alkaline pH values (Bejosano and Corke ; Tomotake and others ; Aluko and Monu ; Silva‐Sanchez and others ; Cordero‐De‐Los‐Santos and others ; Tömösközi and others ; Tang and others ; Bejarano‐Lujan and Netto ; Elsohaimy and others ; Steffolani and others ; Ruiz and others ). Depending on the particular study, very good solubility has also been observed at pH 2.0 (Tomotake and others ; Tang and others ; Shevkani and others ).…”

Section: Techno‐functional Propertiesmentioning

confidence: 98%

“…Amaranth albumins and globulins and proteins extracted under alkaline conditions show similar low solubility at pH values between 3.0 and 5.0. Above pH 5.0, its albumins (maximum solubility of 90% at pH 11.0) are more soluble than its globulins (maximum solubility around 50% at pH 11.0 (Tömösközi and others ). According to Carrazco‐Pena and others (), the amaranth 11S globulins, which are the major proteins of amaranth (Table ), show minimal solubility between pH 2.6 and 4.6 (around 10% and 20% at low and high ionic strength, respectively).…”

Section: Techno‐functional Propertiesmentioning

confidence: 99%

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Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Janssen

Pauly

Rombouts

et al. 2016

Comp Rev Food Sci Food Safe

142

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There is currently much interest in the use of pseudocereals for developing nutritious food products. Amaranth, buckwheat, and quinoa are the 3 major pseudocereals in terms of world production. They contain high levels of starch, proteins, dietary fiber, minerals, vitamins, and other bioactives. Their proteins have well-balanced amino acid compositions, are more sustainable than those from animal sources, and can be consumed by patients suffering from celiac disease. While pseudocereal proteins mainly consist of albumins and globulins, the predominant cereal proteins are prolamins and glutelins. We here discuss the structural properties, denaturation and aggregation behaviors, and solubility, as well as the foaming, emulsifying, and gelling properties of amaranth, buckwheat, and quinoa proteins. In addition, the technological impact of incorporating amaranth, buckwheat, and quinoa in bread, pasta, noodles, and cookies and strategies to affect the functionality of pseudocereal flour proteins are discussed. Literature concerning pseudocereal proteins is often inconsistent and contradictory, particularly in the methods used to obtain globulins and glutelins. Also, most studies on protein denaturation and techno-functional properties have focused on isolates obtained by alkaline extraction and subsequent isoelectric precipitation at acidic pH, even if the outcome of such studies is not necessarily relevant for understanding the role of the native proteins in food processing. Finally, even though establishing in-depth structure-function relationships seems challenging, it would undoubtedly be of major help in the design of tailor-made pseudocereal foods.

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Section: Techno‐functional Propertiesmentioning

confidence: 93%

Section: Techno‐functional Propertiesmentioning

confidence: 98%

Section: Techno‐functional Propertiesmentioning

confidence: 99%

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Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Janssen

Pauly

Rombouts

et al. 2016

Comp Rev Food Sci Food Safe

142

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“…Besides their good amino acid balance, the functional properties of amaranth proteins is important for food processing, and can be modified by extraction processes (Fidantsi & Doxastakis, 2001;Tömösközi et al, 2008). The whole isolate does not exhibit good emulsifying and foaming properties at pH 8.0 (Tömösközi et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

“…The whole isolate does not exhibit good emulsifying and foaming properties at pH 8.0 (Tömösközi et al, 2008). Amaranth albumins (main fraction) have a higher emulsifying activity at pH 5.0 while amaranth globulins exhibit their higher emulsifying properties at pH 7.0 (Silva-Sanchez, GonzalesCastenada, de Leon-Rodriguez & Barba de la Rosa, 2004).…”

Section: Introductionmentioning

confidence: 99%

Interfacial and emulsifying properties of amaranth (Amaranthus hypochondriacus) protein isolates under different conditions of pH

Ventureira

Bolontrade

Speroni

et al. 2012

LWT - Food Science and Technology

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a b s t r a c tAmaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be envisaged to better exploit their potentialities. To better understand their emulsifying properties we have studied their interfacial activities at pHs 2.0 and 8.0 and tried to make the link between 2D and 3D properties.Our results clearly demonstrate the better properties of AI at pH 2.0 than at pH 8 in terms of protein solubility, spreading, adsorption, viscoelastic properties of interfaces and emulsion stability. These results are in relation with the denaturated state of proteins at pH 2.0 where proteins form a harder interfacial film, as compared to pH 8.0. Thus the potential use of amaranth proteins in emulsifying applications should be oriented towards acidic applications.

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Potential of Amaranthus cruentus BRS Alegria in the production of flour, starch and protein concentrate: chemical, thermal and rheological characterization

Tapia‐Blácido

Sobral

Menegalli

2010

J. Sci. Food Agric.

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Functional properties of protein preparations from amaranth seeds in model system

Cited by 24 publications

References 11 publications

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Interfacial and emulsifying properties of amaranth (Amaranthus hypochondriacus) protein isolates under different conditions of pH

Potential of Amaranthus cruentus BRS Alegria in the production of flour, starch and protein concentrate: chemical, thermal and rheological characterization

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