Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins

Molina, Elena; Papadopoulou, Athena; Ledward, D.A.

doi:10.1016/s0268-005x(01)00023-6

Cited by 324 publications

(206 citation statements)

References 38 publications

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“…Partiendo desde valores de pH ácidos, la solubilidad disminuye a medida que el pH va aumentando, hasta que alcanza el punto isoeléctrico, debido a la pérdida de fuerzas de repulsión electrostáticas, lo que proporciona condiciones favorables para la formación de agregados proteicos, la alta densidad aparente y el gran diámetro de los agregados resultan en la precipitación de la proteína, mientras que las fuerzas electrostáticas de repulsión entre las proteínas con carga positiva ayudan a mantenerlas separadas y aumentar las interacciones proteína-solvente y por tanto la solubilidad a valores de pH básicos (Singh et al, 2005). El perfil de solubilidad se emplea como una guía para determinar la funcionalidad de proteínas de diversas fuentes, pues se relaciona directamente con propiedades como la capacidad para formar emulsiones, espumas y geles (Molina, Papadopoulou, & Ledward, 2001;Molina Ortiz & Wagner, 2002).…”

Section: Resultados Y Discusionesunclassified

Propiedades tecnofuncionales y biológicas de harina, aislado y fracciones proteicas mayoritarias de semillas deInga paterno

Sánchez-Mendoza

Ruíz-Ruíz

Dávila-Ortíz

et al. 2017

CyTA - Journal of Food

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RESUMENSe evaluaron las propiedades tecnofuncionales y biológicas de harina, aislado proteico, albúminas y globulinas de semillas de Inga paterno, incluyendo solubilidad proteica, capacidad de absorción de agua y aceite, capacidad espumante y emulsionante, poder reductor de hierro (FRAP) y capacidad inhibitoria de la Enzima Convertidora de Angiotensina (ECA-I). Los resultados muestran que las globulinas presentan mayor solubilidad proteica, capacidad emulsionante y de absorción de aceite; mientras que las albúminas mejor capacidad de absorción de agua, mientras que el aislado proteico mostro mejor capacidad espumante. Estas propiedades fueron dependientes del pH. El FRAP fue de entre 3 y 30% de (0,1-0,3 mg proteína/mL) en todas las muestras, mientras que la actividad de inhibitoria de la ECA-I (0,3 mg proteína/mL) se presentó en harina y aislado proteico, existiendo diferencia estadísticamente significativa (p < 0,05) debido al tratamiento en ambos ensayos. La incorporación de proteínas de semillas de Inga paterno a formulaciones alimenticias podría mejorar sus propiedades tecnofuncionales y su actividad biológica.Techno-functional and biological properties of flour, isolated and majority protein fractions from seeds of Inga paterno ABSTRACT Inga paterno seeds techno-functional and biological properties of flour, protein isolate, albumins and globulins were evaluated. Protein solubility, water and oil absorption capacity, foaming and emulsifying capacity and stability, FRAP and inhibitory capacity ACE-I were including. Globulins had the highest protein solubility, emulsifying capacity and fat absorption capacity; while albumins showed better water absorption capacity. Protein isolate had higher values at foaming capacity. Techno-functional properties were pH dependent. The tested samples showed values between 3 and 30% of FRAP (0.1-0.3 mg protein/mL). Furthermore, flour and protein isolate showed inhibitory activity of ACE-I (0.3 mg protein/mL). Incorporation of Inga paterno proteins seed to food formulations could improve its techno-functional properties and biological activity. ARTICLE HISTORY

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Section: Resultados Y Discusionesunclassified

Propiedades tecnofuncionales y biológicas de harina, aislado y fracciones proteicas mayoritarias de semillas deInga paterno

Sánchez-Mendoza

Ruíz-Ruíz

Dávila-Ortíz

et al. 2017

CyTA - Journal of Food

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“…Consequently, the emulsifying properties of soy proteins are governed by their dispersibilities, surface hydrophobilities and conformational mobilities. The extent of unfolding depends on the available surface area, the amount of time spent in contact with the interface, and the macromolecular structure prior to adsorption [Dickinson, 1993;Molina et al, 2001]. After adsorption at the interface, proteins form a thick interfacial layer to stabilise the emulsion.…”

Section: Soy Protein 31 Soy Proteins and Their Structural And Functimentioning

confidence: 99%

“…Various physical (heat or mild alkali treatments), chemical (acylation, alkylation, oxidation, phosphorylation, and deamidation, etc. ) and enzymatic (transglutaminase, protease, and peptidoglutaminase) methods have been employed to modify the physico-chemical properties and nutritional value of soy proteins [Hamada, 1992, Molina, 2001, Moure, 2006. Chemical approaches have several drawbacks, such as the lack of specificity and the loss of nutritional value.…”

Section: Modification Of Soy Proteinsmentioning

confidence: 99%

Soybean-based Surfactants and Their Applications

Xu¹,

Nakajima²,

Liu³

et al. 2011

Soybean - Applications and Technology

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“…Studies on characterization and functional properties of the proteins glycinin and β-conglycinin in different soybean cultivars were carried out (MOLINA; PAPADOULOS; LEDWARD, 2001, RIBLETT et al, 2001, KHATIB et al, 2002, CARRÃO-PANIZZI et al, 2008. Both fractions are also capable of stimulating activity receptor for low density cholesterol (LDL), (ANTHONY, 2000;ERDMAN, 2000).…”

Section: Introductionmentioning

confidence: 99%

Variation in genetic and environmental effects of beta-conglycinin (7S) and glycinin (11S) protein fractions in conventional and GM soybean cultivars grown in Southern Brazil

et al. 2013

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Efeito de genética e meio ambiente nos teores de frações proteicas beta-conglicinina (7S) e glicinina (11S) em cultivares de soja convencionais e transgênicas cultivadas no sul do BrasilOlívio Fernandes Galão AbstractThe objective of this study was to evaluate the effects of genetic and environmental variation on levels of beta-conglycinin and glycinin in commercial soybean cultivars, which were sown in showcases at Embrapa Soja, Londrina, simultaneously in Ponta Grossa, south Brazil. The concentration of protein fractions was determined by densitometry after electrophoresis in 20 cultivars, 14 conventional and 6 transgenic . We observed a significant variation as the ratio of beta-conglycinin (7S) and glycinin (11S) between the cultivars analyzed. Most 11S/7S ratios (2.21) was observed in the BRS 184, Ponta Grossa and lowest (1.31) in the BRS 233, Londrina. On average, transgenic varieties of Ponta Grossa were higher than in Londrina for both, taking into account the amount of protein fractions. Key words: Soybean, glycinin and beta-conglycinin, protein fractions ResumoO objetivo deste estudo foi avaliar os efeitos de genética e meio ambiente na concentração de beta-conglicinina e glicinina em variedades de soja comercial e que foram cultivadas em fazendas experimentais da Embrapa-soja de Londrina e de Ponta Grossa, no sul do Brasil. A concentração das frações proteicas foi determinada por densitometria após análise por eletroforese em 20 cultivares, sendo 14 convencionais e 6 variedades transgênicas. Foram observadas diferenças significativas na razão de beta-conglicinina (7S) e glicinina (11S) nestas variedades cultivadas. A maior razão 11/7S foi observada na variedade BRS 184 de Ponta Grossa e a menor (1,31) na variedade BRS 233 de Londrina. Em média as variedades transgênicas de Ponta Grossa apresentaram maiores relações que aquelas de Londrina, tendo em conta as quantidades de frações proteicas.

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Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins

Cited by 324 publications

References 38 publications

Propiedades tecnofuncionales y biológicas de harina, aislado y fracciones proteicas mayoritarias de semillas deInga paterno

Propiedades tecnofuncionales y biológicas de harina, aislado y fracciones proteicas mayoritarias de semillas deInga paterno

Soybean-based Surfactants and Their Applications

Variation in genetic and environmental effects of beta-conglycinin (7S) and glycinin (11S) protein fractions in conventional and GM soybean cultivars grown in Southern Brazil

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