Dataset Information

Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions.

ABSTRACT: This research aimed to investigate the possibility of forming gelled nanoemulsions (NEs) by inducing attractive interactions among the nanodroplets. The effect of salt concentration and changes in pH on the stability and gelation behavior of 2, 4, and 5% sodium caseinate (SC) and whey protein isolate (WPI)-stabilized 40% canola oil-in-water NEs were investigated. For the effect of salt, sodium chloride was added in a concentration of 0.1, 0.5, and 1 M in the continuous phase of the NEs at neutral pH, whereas to study the effect of acidification, the pH of the NEs was adjusted to the isoelectric point (pI) of the proteins. The addition of salt led to attractive gelation in WPI NEs because of a screening of charge. In contrast, the gel strength of SC-stabilized NEs was reduced with salt, which was attributed to the loss of close packing of droplets and their surrounding repulsive barriers because of charge screening and to the steric barrier of interfacial SC preventing droplet aggregation. All the NEs with pH at the pI of proteins transformed into strong attractive gels made of droplet aggregates irrespective of the type or concentration of protein because of the complete charge neutralization. The strength of the acidified NE gels increased with a decrease in droplet size and the type of protein used. Overall, research on the effect of different environmental factors on the stability and gelation behavior of protein-stabilized NEs could be useful for possible applications of these nanoscale materials in various food systems.

SUBMITTER: Patel A

PROVIDER: S-EPMC6682039 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions.

Patel Aakash A Longmore Natalie N Mohanan Athira A Ghosh Supratim S

ACS omega 20190708 7

This research aimed to investigate the possibility of forming gelled nanoemulsions (NEs) by inducing attractive interactions among the nanodroplets. The effect of salt concentration and changes in pH on the stability and gelation behavior of 2, 4, and 5% sodium caseinate (SC) and whey protein isolate (WPI)-stabilized 40% canola oil-in-water NEs were investigated. For the effect of salt, sodium chloride was added in a concentration of 0.1, 0.5, and 1 M in the continuous phase of the NEs at neutra ...[more]

PMID: 31460287

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Project description:Deamidation of proteins is one of the most prevalent post-translational modifications found upon aging, and in age-onset diseases. Specific asparagine and glutamine residues are often selectively deamidated during this process. In the human lens, deamidation has been shown to occur in many crystallins, but it is not clear how these deamidated proteins lead to lens opacity or cataract. Here we have modeled in vitro the effect of deamidation of specific asparagine and glutamine residues in human recombinant ?S-crystallin (HGS) on the solution properties of the protein. The residues selected for deamidation in vitro are those that are found to be deamidated in aged and cataractous lenses in vivo. Two derivatives were prepared, one with Asn76 and Asn143 deamidated (2N-HGS) and the other with two additional Gln residues (92 and 120) deamidated (2N2Q-HGS). Isoelectric focusing measurements showed the expected lowering of the pI from 6.9 in HGS to ?6.5 in 2N-HGS and to ?6.1 in 2N2Q-HGS. However, spectroscopic studies showed no significant change in the secondary and tertiary structures of the deamidated proteins relative to the wild type. The stability of 2N-HGS and 2N2Q-HGS, as measured by guanidinium hydrochloride unfolding, also remained comparable to that of HGS. The main difference was the altered protein-protein interaction among the three proteins. The net repulsive interactions that are characteristic of HGS are diminished in the deamidated derivatives as evidenced by static light scattering measurements of the second virial coefficient, B2 (B2 values for HGS, 2N-HGS, and 2N2Q-HGS of 8.90 × 10(-4), 7.10 × 10(-4), and 6.65 × 10(-4) mL mol g(-2), respectively). Further substantiation is provided by estimates of the excess binding energy of protein-protein interactions in the condensed phase, obtained from measurements of the PEG-induced liquid-liquid phase separation profiles for the three proteins. The data suggest that enhanced attractive protein-protein interactions, arising from the deamidation of HGS, promote protein aggregation, thereby leading to increased light scattering and opacity over time.

Dataset Information

Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions.

Publications

Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions.

Similar Datasets

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