Impact of environment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs

Sponton, Osvaldo E.; Pérez, Adrián A.; Carrara, Carlos R.; Santiago, Liliana G.

doi:10.1016/j.foodhyd.2015.02.011

Cited by 63 publications

(30 citation statements)

References 26 publications

(49 reference statements)

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“…The applied strategy consisted of: (i) obtaining BLG-LA complexes via BLG ability for binding LA, and (2) BNP production via HMP electrostatic deposition (attractive electrostatic interaction) onto the surface of pre-formed BLG-LA complexes. LA encapsulation using BNPs is justified due to their high environmental susceptibility in food matrices (Perez, Andermatten, Rubiolo, & Santiago, 2014;Sponton, Perez, Carrara, & Santiago, 2014, 2015a, 2015b. This strategy was reported by Zimet and Livney (2009), supporting the idea that a cover of polysaccharide on the surface of the protein-PUFA complexes could favour the protection of PUFA molecules, mainly against oxidation.…”

Section: Introductionmentioning

confidence: 55%

Biopolymer nanoparticles designed for polyunsaturated fatty acid vehiculization: Protein–polysaccharide ratio study

et al. 2015

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Section: Introductionmentioning

confidence: 55%

Biopolymer nanoparticles designed for polyunsaturated fatty acid vehiculization: Protein–polysaccharide ratio study

et al. 2015

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“…www.nature.com/scientificreports www.nature.com/scientificreports/ The effects of heating on the surface hydrophobicity of OVA and OVA-CMC complexes. Heating would allow protein unfolding and exposition of hydrophobic residues, which was beneficial for the increasing of interfacial activity 15,16 . H 0 value of OVA was decreased after binding with CMC ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Improving emulsion stability based on ovalbumin-carboxymethyl cellulose complexes with thermal treatment near ovalbumin isoelectric point

Kuang

Jiang

et al. 2020

Sci Rep

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Ovalbumin (OVA) is an important protein emulsifier. However, it is unstable near the isoelectric point pH, which limits its applications in the food industry. Polysaccharides may be explored to tackle this challenge by improving its pH-dependent instability. In this work, carboxymethyl cellulose (CMC) was used as a model polysaccharide to mix with OVA near its isoelectric point (pH 4.7) with subsequent mild heating at 60 °C for 30 min. The molecular interactions between OVA and CMC were comprehensively studied via a series of characterizations, including turbidity, zeta potential, intrinsic fluorescence, surface hydrophobicity, circular dichroism (CD) spectra and Fourier transform infrared spectroscopy (FTIR). The droplet sizes of the emulsions prepared by OVA-CMC were measured to analyze emulsifying property and stability. The results indicated that free OVA was easily aggregated due to loss of surface charges, while complexing with CMC significantly inhibited OVA aggregation before and after heating owing to the strong electrostatic repulsion. In addition, OVA exposed more hydrophobic clusters after heating, which resulted in the growth of surface hydrophobicity. Altogether, the heated OVA-CMC complexes presented the best emulsifying property and stability. Our study demonstrated that complexing OVA with CMC not only greatly improved its physicochemical properties but also significantly enhanced its functionality as a food-grade emulsifying agent, expanding its applications in the food industry, as development of emulsion-based acidic food products.Egg ovalbumin (OVA), the main ingredient of egg white protein, is one of the most widely used protein and a kind of important food ingredient. In addition, OVA also possesses important functionalities including emulsifying and foaming stability because it has more than 50% hydrophobic amino acids, similar to other surface-active agents 1,2 . Nevertheless, there are two major limitations for OVA to be widely used in the food industry. First, OVA is known to have poor thermal instability. It was reported that the thermal aggregation temperature of OVA was lower around its isoelectric point than that in other pH conditions, and the optimal thermal stability was in the pH range from 6 to 10 3,4 . In addition, the emulsifying property of OVA was poor near the isoelectric point as shown in our previous work 2 . Meanwhile, as a protein molecule, when the pH is reduced to around its isoelectric point (pH 4.7), OVA carries zero net surface charge and loses its emulsifying capability when used in the emulsion-based acidic food products, such as yogurt and lactic acid beverages 5 .Carboxymethyl cellulose (CMC), one of the derivatives of cellulose, has been widely used as a stabilizing agent in foods 6 . In addition, CMC is stable with strong negative charges at pH values from 2 to 10, which makes it suitable for various applications in most food products across a wide range of pH conditions. CMC is a commonly used additive to improve the processing properties of products in cos...

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“…When the pH was close to the isoelectric point, the maximum absorption wavelength of each sample was blueshifted SPI, SPI-D SPH-D was 340.8, 343.4, 343.8 nm at pH 5.0, respectively , indicated that the protein was polymerized near the isoelectric point, and the maximum absorption wavelength was red-shifted as the pH away from isoelectric point, shifted by 3.4, 3.8, 3.8 nm at pH 9.0, respectively, the molecules were turned on. However, SPI-D was significantly red-shifted compared to SPI alone at the same pH, indicated that the glycation reaction changed the surrounding environment of the protein tryptophan residue, and the tryptophan residue was exposed to a more hydrophilic environment 31 . At the same time, it could also be seen that SPH-D was more red-shifted, indicated that enzymatic hydrolysis could unfold the SPI structure and be exposed by the internal tryptophan group to increase its surface hydrophobicity 32 .…”

Section: Endogenous Uorescence Spectrometrymentioning

confidence: 99%

Effect of pH on Freeze-thaw Stability of Glycated Soy Protein Isolate

et al. 2019

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Introduction Many proteins are used as high-efficiency emulsifiers because they contain both hydrophobic and charged hydrophilic regions, which reduce the surface tension and interact at the emulsions interface 1 , they are widely used in food, nutrition, and pharmaceutical industries. In order to maintain microbiological and chemical stability and extending the shelf life of food products, freezing becomes one of the most important preservation methods. When the emulsions are stored at 20 , a variety of phenomenon can occur including creaming, sedimentation, oiling off and phase separation of the emulsions 2 , which limit its application in the food industry. And protein emulsions stability is sensitive to environmental stress, such as pH, ionic strength, and temperature 3. Degner et al. 4 reported that the freeze-thaw instability of emulsions was mainly related to the crystallization of oil-water phase and the change in droplet microenvironment conditions pH, viscosity, osmotic pressure and ionic strength. Both proteins and polysaccharides play an important role in terms of structure and stability 5. Polysaccharides and proteins can be used in the preparation of edible film applications in the food field 6. Polysaccharides can also act as catalysts to promote the amination of 1,2-epoxycyclohexane 7. In addition, polysaccharides can be used in the medical field due to their biological activity 8. The enhanced emulsifying properties of protein-polysaccharide

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Impact of environment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs

Cited by 63 publications

References 26 publications

Biopolymer nanoparticles designed for polyunsaturated fatty acid vehiculization: Protein–polysaccharide ratio study

Biopolymer nanoparticles designed for polyunsaturated fatty acid vehiculization: Protein–polysaccharide ratio study

Improving emulsion stability based on ovalbumin-carboxymethyl cellulose complexes with thermal treatment near ovalbumin isoelectric point

Effect of pH on Freeze-thaw Stability of Glycated Soy Protein Isolate

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