Eigenschaften von Eiweißstoffen in Komplexen mit sauren Polysacchariden und anderen Polyelektrolyten

Strelzowa, S. A.; Tolstogusow, W. B.

doi:10.1007/bf01549892

Cited by 15 publications

(4 citation statements)

References 33 publications

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“…Apparently, there is little or no structural disruption caused by complexation with PDADMAC. Unchanged CD spectra were also observed for complexes formed with ferrihemoglobin and PAMPS or NVP-AMPS (data not shown), and similar results were described by Strelzowa et al 32 for ␦-chymotrypsin with dextran sulfate. However, the absence of structural perturbation upon complexation should not be considered as universal.…”

Section: Of Ferrihemoglobin-polyelectrolyte Complexessupporting

confidence: 88%

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

et al. 1999

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Quasi-elastic light scattering (QELS), electrophoretic light scattering (ELS), CD spectroscopy, and azide binding titrations were used to study the complexation at pH 6.8 between ferrihemoglobin and three polyelectrolytes that varied in charge density and sign. Both QELS and ELS show that the structure of the soluble complex formed between ferrihemoglobin and poly(diallyldimethylammonium chloride) [PDADMAC] varies with protein concentration. At fixed 1.0 mg/mL polyelectrolyte concentration, protein addition increases complex size and decreases complex mobility in a tightly correlated manner. At 1.0 mg/mL or greater protein concentration, a stable complex is formed between one polyelectrolyte chain and many protein molecules (i.e., an intrapolymer complex) with apparent diameter approximately 2.5 times that of the protein-free polyelectrolyte. Under conditions of excess polyelectrolyte, each of the three ferrihemoglobin-polyelectrolyte solutions exhibits a single diffusion mode in QELS, which indicates that all protein molecules are complexed. CD spectra suggest little or no structural disruption of ferrihemoglobin upon complexation. Azide binding to the ferrihemoglobin-poly(2-acrylamide-2-methylpropanesulfonate)

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Section: Of Ferrihemoglobin-polyelectrolyte Complexessupporting

confidence: 88%

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

et al. 1999

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“…This is due to suppression of the dissociation of the enzyme's side chain ionizable groups in the micro-environment of an anionic polysaccharide. 15 Generally, in the complexed state, renaturation or refolding of the denatured protein is inhibited. 10,17,28 An example of this is the irreversibility of thermal denaturation of the Kunitz trypsin inhibitor bound to anionic polysaccharides and other proteins.…”

Section: Control Of Enzymes and Enzyme Inhibitorsmentioning

confidence: 99%

“…At high salt concentration these complexes are dissociated. 5,15,16,26 Since the composition and properties of a complex depend on its formation conditions, e.g. on the way of their preparation and the time of aging, interbiopolymer complexes can be not at equilibrium.…”

Section: Macromolecular Ingredient Interactions 721 Basic Principlesmentioning

confidence: 99%

Ingredient interactions in complex foods: aggregation and phase separation

Tolstoguzov¹

2007

Understanding and Controlling the Microstructure of Complex Foods

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“…It was found [41,42] that the activity of enzymes bound in complexes with anionic polysaccharides is retained, but the pH optimum is shifted to lower pH values. This change in pH optima due to the change in the protein charge within the electrostatic field of the polysaccharide, could be of importance for the protection (against proteolytic attack) of the alimentary canal walls, i. e. the protection of the mucus membrane lining (immobilizing enzymes and antibacterial proteins and acting as the non-specific barrier of internal medium) against self digestion.…”

Section: Some Thermodynamic Aspects Of Digestion and Non-specific Immmentioning

confidence: 99%

Phase behaviour of macromolecular components in biological and food systems

Tolstoguzov¹

2000

Nahrung

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Reasons for the greatly different phase behaviour of: (i) biological systems (cytoplasm of the cell), (ii) food systems and (iii) beverages are considered. The two phenomena: molecular mimicry and molecular symbiosis presumably control thermodynamic compatibility of biological macromolecules. The three interacting factors underlying molecular mimicry, are: (i) low excluded volume of densely packed protein globules, (ii) chemical resemblance of surfaces of the globules and (iii) the chemical information hidden in the hydrophobic interior of the globules. The symbiotic relationship presumably exists between rod-like macromolecules and protein globules, i.e. between macromolecules of the two extreme conformations typical of biopolymers. For instance, thermodynamic activity of an enzyme can be controlled by dissociation-association of rod-like macromolecules. Due to excluded volume effects, biopolymers behave as if they were in a solution of a higher concentration. Both molecular mimicry and molecular symbiosis could also be of importance for non-specific immune defence, digestion of proteins and formation of food structures. Unlike biological systems, thermodynamic incompatibility is typical of foods and still more of beverages. Denaturation, aggregation and complexing of food macromolecules decrease their mimicry and co-solubility. Due to their relatively low viscosity and high chemical and physical heterogeneity of macromolecules, the phase behaviour of beverages is similar to that of mixed solutions of synthetic polymers. Phase separation of biopolymer mixtures is of importance for controlling composition-property relationship in formulated food and drinks.

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Eigenschaften von Eiweißstoffen in Komplexen mit sauren Polysacchariden und anderen Polyelektrolyten

Cited by 15 publications

References 33 publications

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

Light scattering, CD, and ligand binding studies of ferrihemoglobin-polyelectrolyte complexes

Ingredient interactions in complex foods: aggregation and phase separation

Phase behaviour of macromolecular components in biological and food systems

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