Denaturation of soy proteins in solution and at the oil–water interface: A fluorescence study

Miriani, M.; Keerati-u-rai, Maneephan; Corredig, Milena; Iametti, Stefania; Bonomi, Francesco

doi:10.1016/j.foodhyd.2010.07.020

Cited by 76 publications

(35 citation statements)

References 31 publications

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“…Carp, Bartholomai, and Pilosof (1999) found that the presence of xanthan gum could affect the capacity of different soy protein subunits to adsorb at the aireoil interface in foams. As well, Miriani, Keerati-u-rai, Corredig, Iametti, and Bonomi (2011) found that upon binding to an oilewater interface, b-conglycinin underwent partial unfolding so that its hydrophobic and hydrophilic moieties maximized interactions with the oil and water phases, respectively. This improved the protein's resistance to heat denaturation.…”

Section: Emulsion Morphologymentioning

confidence: 93%

Stabilization of acidic soy protein-based dispersions and emulsions by soy soluble polysaccharides

Tran¹,

Rousseau²

2013

Food Hydrocolloids

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Section: Emulsion Morphologymentioning

confidence: 93%

Stabilization of acidic soy protein-based dispersions and emulsions by soy soluble polysaccharides

Tran¹,

Rousseau²

2013

Food Hydrocolloids

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“…Tandag et al () also reported positive correlation between the content of α′ subunit with ESI. Miriani, Keerati‐u‐rai, Corredig, Iametti, and Bonomi () explained positive influence of α′ and α subunits on emulsion properties through exposure of hydrophobic tryphtophan residues, located in extension regions, on the surface of protein. Since content α and α′ subunits were also positively correlated with solubility at pH 6 and 8, it would be logical to assume that solubility and ESI values were positively correlated at these pH values.…”

Section: Resultsmentioning

confidence: 99%

Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing β' Subunit

Pavlićević

Tomić

Djonlagić

et al. 2018

J Americ Oil Chem Soc

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The effects of subunit composition of two major proteins of soybean: glycinin (11S) and β-conglycinin (7S) in nine different genotypes, on solubility and emulsifying and gelling properties at different pH (3, 5, 6, and 8) were examined. High-protein genotypes (more than 40%) contained low amounts of the β 0 subunit. The main factors influencing solubility at pH 6 were the content of α 0 , α (r = 0.89 and r = 0.91 at P < 0.05, respectively) and β 0 subunit contents (r = −0.71 at P < 0.05) of β-conglycinin, while at pH 3 acidic subunits in glycinin had a positive correlation with solubility (r = 0.69 at P < 0.05). Emulsion activity at pH 6 was higher for genotypes synthesizing β 0 subunit (r = 0.57 at P < 0.05). Genotypes synthesizing higher amounts of α 0 and α subunit had higher emulsion stability at pH 6 (r = 0.85 and r = 0.92 at P < 0.05, respectively) and pH 8 (r = 0.91 and r = 0.97 at P < 0.05, respectively). The rheological measurements showed that genotypes with 11S/7S ratio higher than 2.2 formed gels with enhanced storage moduli. This influence was largely due to the high content of SH groups in glycinin acidic polypeptides resulting in stabilization of gels via disulfide bonding. Gels prepared from genotypes containing higher amounts of β 0 subunit of β-conglycinin exhibited reduced elastic properties. Genotypes showing better solubility also had higher emulsion stability, but formed weaker gels and had lower emulsion activity near neutral pH.Keywords Soybean proteins Á β 0 subunit Á Solubility Á Emulsion properties Á Gelling properties J Am Oil Chem Soc (2018) 95: 123-134.

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“…Shifts in the emission maxima of tryptophan fluorescence have been utilized to evaluate structural changes at the oil-water interface of soy-protein stabilized emulsions [38,39] before and after heat treatments. Fluorescent molecular rotors have been proposed to study stability of colloidal systems [23 ,40] and the fluorescence intensity of a presumptive GRAS molecular rotor, yellow #6 (sunset yellow FCF) was recently used to evaluate formation of surfactant assemblies [41].…”

Section: Gras Probes Of Microstructural Organizationmentioning

confidence: 99%

Making sense of luminescence from GRAS optical probes

Corradini

Ludescher

2015

Current Opinion in Food Science

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Denaturation of soy proteins in solution and at the oil–water interface: A fluorescence study

Cited by 76 publications

References 31 publications

Stabilization of acidic soy protein-based dispersions and emulsions by soy soluble polysaccharides

Stabilization of acidic soy protein-based dispersions and emulsions by soy soluble polysaccharides

Evaluation of Variation in Protein Composition on Solubility, Emulsifying and Gelling Properties of Soybean Genotypes Synthesizing β' Subunit

Making sense of luminescence from GRAS optical probes

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