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

Antonov, Yu. A.; Dmitrochenko, A. P.; Leontiev, A.L.

doi:10.1016/j.ijbiomac.2005.12.011

Cited by 9 publications

(4 citation statements)

References 34 publications

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“…Ducel, Food Research International 44 (2011) 1441-1446Saulnier, Richard, and Boury (2005 and Chourpa, Ducel, Richard, Dubois, and Boury (2006) investigated the structural changes involved with the complexation of pea globulin and α-gliadin with gum Arabic, to confirm pH-induced conformational perturbations of the secondary protein structure upon complexation. Complexation has also been investigated for other plant-based systems such as, alfalfa rubisco and pectin (Antonov & Soshinsky, 2000), and faba bean 11 S globulin and carboxyl methylcellulose (Antonov, Dmitrochenko, & Leontiev, 2006).…”

Section: Introductionmentioning

confidence: 99%

Complex coacervation in pea protein isolate–chitosan mixtures

Elmer

Karaça

Low

et al. 2011

Food Research International

115

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Section: Introductionmentioning

confidence: 99%

Complex coacervation in pea protein isolate–chitosan mixtures

Elmer

Karaça

Low

et al. 2011

Food Research International

115

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“…The results obtained (Figures and ) show the presence of the intermacromolecular interactions between SC and DSS. Usually coulomb protein−polysaccharide complexes are formed only in the vicinity of the isoelectric point of the protein, but for several systems, formation of soluble protein−polysaccharide complexes has been registered even at pH 6−8.0. − A beneficial consequence of complexation of sulfated polysaccharide with caseins at pH values above IEP is the protection afforded against loss of solubility as a result of protein aggregation during heating or following high-pressure treatment. , The mechanism of this protection has been unclear until now. Snoeren, Payens, Jevnink, and Both assumed that there is a nonstatistical distribution of positively charged amino acid residues along the polypeptide chain of kappa casein molecules and, as a consequence, the existence of a dipole interacting by its positive pole with sulfur polysaccharide is responsible for complex formation in such systems.…”

Section: Resultsmentioning

confidence: 99%

“…Usually coulomb proteinpolysaccharide complexes are formed only in the vicinity of the isoelectric point of the protein, 44 but for several systems, formation of soluble protein-polysaccharide complexes has been registered even at pH 6-8.0. [45][46][47] A beneficial consequence of complexation of sulfated polysaccharide with caseins at pH values above IEP is the protection afforded against loss of solubility as a result of protein aggregation during heating or following high-pressure treatment. 48,49 The mechanism of this protection has been unclear until now.…”

Section: Intermacromolecularmentioning

confidence: 99%

Inducing Demixing of Semidilute and Highly Compatible Biopolymer Mixtures in the Presence of a Strong Polyelectrolyte

Antonov

Moldenaers

2009

Biomacromolecules

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The weak intermacromolecular interactions caused by the presence of a complexing agent in a two-phase biopolymer mixture can affect its phase equilibrium and morphology. In this communication, the attempt was made to induce demixing in semidilute and highly compatible sodium caseinate/sodium alginate system (SC-SA) mixtures in the presence of a sodium salt of dextran sulfate (DSS) at pH 7.0 (above the isoelectrical point of caseins), and to characterize phase equilibrium, intermacromolecular interactions, and structure of such systems by rheo-small angle light scattering (SALS), optical microscopy (OM), phase analysis, dynamic light scattering (DLS), fast protein liquid chromatography (FPLC), ESEM, and rheology. Addition of dextran sulfate sodium salt (DSS) to the semidilute single-phase SC-SA system, even in trace concentrations (10(-3) wt %), leads to segregative liquid-liquid phase separation and a substantial increase in storage and loss moduli of the system. The degree of the protein conversion in the complex grows when the concentration of SC in the system increases from 1 to 2 wt %. It is also established here that demixing of semidilute biopolymer mixtures, induced by the minor presence of DSS, is a rather common phenomenon, because it also was observed here for other biopolymer pairs. At high shear rates SC becomes even less compatible with SA in the presence of DSS than at rest. Experimental observations suggest that the approach for inducing demixing of semidilute and highly compatible biopolymer mixtures by physical interactions of the constituents is a promising tool for regulation of biopolymer compatibility and achieving better predictions of phase behavior of aqueous protein-charged polysaccharide systems.

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“…The binding of proteins to nucleic acids, which are natural polyelectrolyte, is an integral step in gene regulation [1,7,8]. A weak intermacromolecular interactions are responsible for a dramatically changes in thermodynamic compatibility of biopolymers [9][10][11]. Intermacromolecular interactions can be utilized for isolation of proteins [4,5,12] and enzymes [13], enzyme immobilization [3,14], encapsulation [15] and drug delivery [14,16].…”

Section: Introductionmentioning

confidence: 99%