The factors affecting the compatibility of serum albumin and pectinate in aqueous medium

Семенова, М.Г.; Bolotina, V.S.; Dmitrochenko, A. P.; Leontiev, A.L.; Polyakov, Vyacheslav; Braudo, E. E.; Tolstoguzov, V. B.

doi:10.1016/0144-8617(91)90088-t

Cited by 33 publications

(9 citation statements)

References 17 publications

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“…According to Albano and Telis [37] these systems did not show visual phase separation, indicating biopolymers' miscibility, which occur more in diluted solutions with low concentration of macromolecules. There are a few casesfor example, blends of whey albumin and pectin [38], in which a genuine and complete miscibility in non-diluted dispersions of two biopolymers has been observed [10].…”

Section: Zeta Potential and Turbidimetrymentioning

confidence: 99%

Ultrasound impact on whey protein concentrate-pectin complexes and in the O/W emulsions with low oil soybean content stabilization

Albano

Telis

2018

Ultrasonics Sonochemistry

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Consumers' preference for products with reduced levels of fat increased in the last years. Proteins and polysaccharides have an important role due to their functional and interaction properties because, when combined in ratios and pH of higher potential for electrostatic interactions they may act as emulsifiers or stabilizers. This study evaluated the ultrasound impact on the electrostatic interaction between pectin (PEC) and whey protein concentrate (WPC) at different WPC:PEC ratios (1:1 to 5:1), and its effect on the emulsification and stability of emulsions formulated with WPC:PEC blends (1:1, 4:1) at low soybean oil contents (5 to 15%). Zeta potential analysis showed greater interactions between biopolymers at pH 3.5, which was proven in FTIR spectra. Rheology and turbidimetry showed that the ultrasound reduced the suspension viscosity and the size of the biopolymer complexes. Suspensions were Newtonian, whereas the emulsions showed shear-thinning behavior with slight increase in apparent viscosity as a function of oil content, and remained stable for seven days, with small droplets (<8 μm) stabilized and entrapped in a pectin network evidenced by confocal laser microscopy. Sonication was successfully applied to emulsion stabilization, improving the functional properties of WPC:PEC blends and enabling their application as low-fat systems, providing healthier products to consumers.

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Section: Zeta Potential and Turbidimetrymentioning

confidence: 99%

Ultrasound impact on whey protein concentrate-pectin complexes and in the O/W emulsions with low oil soybean content stabilization

Albano

Telis

2018

Ultrasonics Sonochemistry

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“…The estimated experimental error was about 5-7%. The dependence of viscosity of the CMC solutions on concentration was determined in coordinates of the Fuoss' expression [35].…”

Section: Methodsmentioning

confidence: 99%

Interactions and compatibility of 11 S globulin from Vicia Faba seeds and sodium salt of carboxymethylcellulose in an aqueous medium

Antonov

Dmitrochenko

Leontiev

2006

International Journal of Biological Macromolecules

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“…The influence of the pectin structure on the thermodynamic compatibility with proteins was examined by Semenova et al [11], using human serum albumin and by Antonov et al [12] using gelatine. In both studies the influence of pH, ionic strength, temperature and the degree of esterification (DE) of the pectin was tested.…”

Section: Introductionmentioning

confidence: 99%

“…In both studies the influence of pH, ionic strength, temperature and the degree of esterification (DE) of the pectin was tested. The pectins of different DE were prepared by alkaline demethylation [12] or fractionation [11].…”

Section: Introductionmentioning

confidence: 99%

“…Antonov et al [12] found an increasing compatibility for pectins and gelatine with increasing DE of the pectin component at pH 6.0 and an ionic strength of 0.5 M NaCl. Semenova et al [11] observed a higher affinity of the serum albumin to pectin with decreasing DE at pH 7 and 0.1 M ionic strength. Maroziene and de Kruif [8] noticed a variation in the binding of pectins with varying DE and degree of amidation (DA) to casein micelles.…”

Section: Introductionmentioning

confidence: 99%

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Thermodynamic compatibility of sodium caseinate with different pectins. Influence of the milieu conditions and pectin modifications

Einhorn-Stoll¹,

Salazar

Jaafar

et al. 2001

Nahrung

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Combinations of pectins and caseins are ingredients of many food products. Therefore the thermodynamic compatibility of both components was examined to investigate the influences of environmental factors as well as of the structure of the pectin. High-methoxyl pectin was demethoxylated and amidated, respectively, and tested for the compatibility with sodium caseinate under varying conditions of pH and ionic strength. The compatibility increased with increasing pH and decreasing ionic strength. Demethoxylated pectins were more and amidated pectins less compatible with the caseinate. Changes in the pectin hydrophilicity, solubility and molecular weight and possibly local interactions such as electrostatic attraction, hydrogen bonding and calcium bridges are involved in the compatibility of the components. The type and degree of the pectin modifications as well as the type, composition and properties of the protein were found to be of great importance for the thermodynamic compatibility.

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The factors affecting the compatibility of serum albumin and pectinate in aqueous medium

Cited by 33 publications

References 17 publications

Ultrasound impact on whey protein concentrate-pectin complexes and in the O/W emulsions with low oil soybean content stabilization

Ultrasound impact on whey protein concentrate-pectin complexes and in the O/W emulsions with low oil soybean content stabilization

Interactions and compatibility of 11 S globulin from Vicia Faba seeds and sodium salt of carboxymethylcellulose in an aqueous medium

Thermodynamic compatibility of sodium caseinate with different pectins. Influence of the milieu conditions and pectin modifications

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