Relationship between the Method of Obtention and the Structural and Functional Properties of Soy Proteins Isolates. 1. Structural and Hydration Properties

Petruccelli, Silvana; Añón, Marı́a Cristina

doi:10.1021/jf00046a017

Cited by 120 publications

(93 citation statements)

References 17 publications

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“…Despite having sulfhydryl (SH) residues, the 7S polypeptides seem to be capable of forming aggregates. This observation had already been reported by Petruccelli and Añón [10,20].…”

Section: Effect Of Acid Treatment On Interfacial and Foam Properties supporting

confidence: 85%

“…The soy proteins were extracted from the supernatant by isoelectric precipitation at pH 4.5. Then, the precipitate was dispersed in an alkaline solution (pH 8.0) and freeze-dried for storage [10].…”

Section: Spi and 7s And 11s Fractionsmentioning

confidence: 99%

“…The SPIn, SPIt, 11Sn, 11St, 7Sn and 7St sample solutions were separated by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) in 7%-15% gradient gels under reducing and non-reducing conditions (with or without β-mercaptoethanol), using a BIO-RAD Mini-PROTEAN ® II equipment as described by Petruccelli and Añón [10]. The runs were conducted at a 90 V constant voltage on two gels (1.0 mm of thickness) in a Hoefer SE640 electrophoresis unit.…”

Section: Electrophoresismentioning

confidence: 99%

“…The molecular weight of each protein was estimated by a Pharmacia low molecular weight (LMW) standard consisting of six proteins, whose molecular weights were 14.4, 20.1, 30.0, 45.0, 66.0 and 97.0 kDa, respectively. The gels were stained with Coomasie blue R-250 as described by Petruccelli and Añón [10].…”

Section: Electrophoresismentioning

confidence: 99%

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Effect of Acid Treatment on Interfacial and Foam Properties of Soy Proteins

Abirached¹,

Medrano²,

Moyna³

et al. 2015

JFSE

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Abstract:The goal of the present work was to study the effects of acid treatment on the foaming properties of a soybean protein isolate (SPI) and its fractions, glycinin (11S) and β-conglycinin (7S). The structural characteristics, interfacial properties, foaming capacity and stability of the treated proteins were studied. Results from surface hydrophobicity and differential scanning calorimetry (DSC) showed that the acid treatment caused the complete denaturation of 11S and a partial denaturation of 7S. This protein unfolding affected their interfacial properties, which led to an improvement in the foaming properties of both protein fractions and isolate. Treated 7S showed the best behavior in the rearrangement process, probably due to its smaller size and its modified structural characteristics. All treated proteins showed stronger interfacial films. The foams of treated proteins were destabilized mostly due to gravitational drainage rather than Ostwald ripening.

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“…Despite having sulfhydryl (SH) residues, the 7S polypeptides seem to be capable of forming aggregates. This observation had already been reported by Petruccelli and Añón [10,20].…”

Section: Effect Of Acid Treatment On Interfacial and Foam Properties supporting

confidence: 85%

Section: Spi and 7s And 11s Fractionsmentioning

confidence: 99%

Section: Electrophoresismentioning

confidence: 99%

Section: Electrophoresismentioning

confidence: 99%

See 2 more Smart Citations

Effect of Acid Treatment on Interfacial and Foam Properties of Soy Proteins

Abirached¹,

Medrano²,

Moyna³

et al. 2015

JFSE

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“…SPI was extracted from the defatted soybean flour according to the reported method (Petruccelli & Anon, 1994). An alkaline extract (pH 8.0) separated from the defatted soybean flour was adjusted to an isoelectric precipitation (pH 4.5) at ambient temperature by adding 2 mol/L HCl.…”

Section: Sample Preparationmentioning

confidence: 99%

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

Zhu

Liu

et al. 2015

CyTA - Journal of Food

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Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan Cambios en la estructura y en las propiedades del aislado de proteína de soja como resultado de la glicación y reticulación mediante transglutaminasa y chitosán degradado A glycated and cross-linked soybean protein isolate (GC-SPI) with the glucosamine content of 19.40 g/kg protein was prepared by using SPI, transglutaminase, and a degraded chitosan under fixed conditions, aiming to assess modified properties and potential application of GC-SPI. GC-SPI has less reactable -NH 2 groups than SPI (0.38 versus 0.48 mol/kg protein), and is verified by electrophoretic analysis to be a glycated and cross-linked protein product. Infrared spectroscopy and circular dichroism analyses demonstrate that GC-SPI contains more -OH groups, and has a more open secondary structure. In comparison with SPI, GC-SPI has higher surface hydrophobicity but lower in vitro digestibility due to protein cross-linking, and exhibits greater water-and oil-binding capacities (9.9 versus 6.4 and 3.7 versus 2.0 kg/kg protein). It is concluded that the glycation and cross-linking confer an open structure and modified properties of SPI, and GC-SPI is a potential ingredient with better hydration and oil-binding than SPI.Keywords: soybean protein isolate; degraded chitosan; transglutaminase; secondary structure; property Se preparó aislado de proteína de soja glicada y reticulada (GC-SPI) con un contenido de glucosamina de 19,40 g/kg de proteína utilizando SPI, transglutaminasa y chitosán degradado sometido a condiciones determinadas con el objetivo de estudiar las propiedades modificadas y las aplicaciones potenciales de GC-SPI. GC-SPI obtuvo menos grupos reactivos de tipo NH 2 en comparación con SPI (0,38 frente a 0,48 mol/kg de proteína) y se verificó mediante análisis electroforético para ser un producto proteínico glicado y reticulado. La espectroscopía infrarroja y el análisis de dicroísmo circular mostraron que el GC-SPI contiene más grupos OH y tiene una estructura secundaria más abierta. En comparación con SPI, GC-SPI tiene una mayor superficie de hidrofobia aunque una menor digestibilidad in vitro debido a la reticulación proteínica, además exhibe una mayor capacidad de retención de agua y de aceite (9,9 frente a 6,4 y 3,7 frente a 2,0 kg/kg de proteína). En conclusión, la glicación y la reticulación conceden una estructura abierta y unas propiedades modificadas en SPI. Además GC-SPI se trata de un ingrediente potencial con una mejor hidratación y capacidad de retención que SPI.Palabras clave: aislado de proteína de soja; chitosán degradado; transglutaminasa; estructura secundaria; propiedad

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Fibers from soybean protein and poly(vinyl alcohol)

Zhang

Ghasemzadeh

Kotliar

et al. 1999

J. Appl. Polym. Sci.

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Bicomponent fibers were wet-spun from soybean protein and poly (vinyl alcohol). The protein core of the spun bicomponent fiber was brittle and showed a high frequency of core breakage upon drawing. Our effort was then to study the soybean protein solution, with the aim of trying to understand the cause for fiber brittleness and to determine the optimum solution conditions for fiber spinning. The effects of alkali, urea, and sodium sulfite on the viscosity of the soybean protein solution were examined. The hydrolytic stability of the soybean protein solution was examined at various pH values at two temperatures (room temperature and 60°C). Both the viscosity and gel electrophoresis were used for this purpose. The degradation of the soybean protein and the existing microgels in the protein spinning solution were thought to be the causes for the poor fiber drawability. Extent of protein denaturation will also effect the fiber drawability.

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Relationship between the Method of Obtention and the Structural and Functional Properties of Soy Proteins Isolates. 1. Structural and Hydration Properties

Cited by 120 publications

References 17 publications

Effect of Acid Treatment on Interfacial and Foam Properties of Soy Proteins

Effect of Acid Treatment on Interfacial and Foam Properties of Soy Proteins

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

Fibers from soybean protein and poly(vinyl alcohol)

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