Protein‐polysaccharide complexes as surfactants

Gurov, A. N.; Nuss, P. V.

doi:10.1002/food.19860300337

Cited by 17 publications

(4 citation statements)

References 2 publications

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“…Where a protein and highly charged polysaccharide are introduced simultaneously, the formation of an electrostatic complex between the two biopolymers can be expected to affect the steps of diffusion, adsorption, and reorganization to differing extents. For example, the adsorption of bovine serum albumin−dextran sulfate (BSA−DS) complexes at the oil−water interface has been reported to take place in two stages: diffusion and rearrangement of the complexes, with a substantially longer diffusion stage. Ganzevles and co-workers have reported much slower diffusion of β-lactoglobulin−pectin complexes at the air−water interface because of the greater hydrodynamic radius of the complexes compared to the pure protein.…”

Section: Introductionmentioning

confidence: 99%

Mixed Layers of Sodium Caseinate + Dextran Sulfate: Influence of Order of Addition to Oil−Water Interface

et al. 2009

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We report on the interfacial properties of electrostatic complexes of protein (sodium caseinate) with a highly sulfated polysaccharide (dextran sulfate). Two routes were investigated for preparation of adsorbed layers at the n-tetradecane−water interface at pH = 6. Bilayers were made by the layer-by-layer deposition technique whereby polysaccharide was added to a previously established protein-stabilized interface. Mixed layers were made by the conventional one-step method in which soluble protein−polysaccharide complexes were adsorbed directly at the interface. Protein + polysaccharide systems gave a slower decay of interfacial tension and stronger dilatational viscoelastic properties than the protein alone, but there was no significant difference in dilatational properties between mixed layers and bilayers. Conversely, shear rheology experiments exhibited significant differences between the two kinds of interfacial layers, with the mixed system giving much stronger interfacial films than the bilayer system, i.e., shear viscosities and moduli at least an order of magnitude higher. The film shear viscoelasticity was further enhanced by acidification of the biopolymer mixture to pH = 2 prior to interface formation. Taken together, these measurements provide insight into the origin of previously reported differences in stability properties of oil-in-water emulsions made by the bilayer and mixed layer approaches. Addition of a proteolytic enzyme (trypsin) to both types of interfaces led to a significant increase in the elastic modulus of the film, suggesting that the enzyme was adsorbed at the interface via complexation with dextran sulfate. Overall, this study has confirmed the potential of shear rheology as a highly sensitive probe of associative electrostatic interactions and interfacial structure in mixed biopolymer layers.

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Section: Introductionmentioning

confidence: 99%

Mixed Layers of Sodium Caseinate + Dextran Sulfate: Influence of Order of Addition to Oil−Water Interface

et al. 2009

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“…Burgess () reported that the high viscosity of albumin–gum arabic coacervate was responsible for producing capsules that were fairly stable against coalescence, even in the absence of cross‐linkers. It was shown, as early as 1980s, that the formation of complex coacervate between bovine serum albumin and dextrane sulfate resulted into increased shear strength of films formed at the liquid interface (Gurov & Nuss, ). Thomassin, Merkle, and Gander () also found that the encapsulation process is influenced by the viscoelasticity of the coacervate.…”

Section: Introductionmentioning

confidence: 99%

Rheological and Microstructural Characteristics of Canola Protein Isolate−Chitosan Complex Coacervates

Chang

Gupta

Timilsena

2019

Journal of Food Science

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Wastage of byproducts such as canola meal is a pressing environmental concern, and canola protein isolate (CPI)−chitosan (Ch) coacervates have a good potential to utilize and convert the wastes into a high value added product. Yet so far, there is very limited rheological and microstructural information to assist in proper utilization of CPI -Ch complex coacervates. The rheological and microstructural properties of the complex coacervates formed from CPI and chitosan Ch at various CPI-to-Ch mixing ratios (1:1, 16:1, 20:1, and 30:1) and pH values (5.0, 6.0, and 7.0) were therefore investigated. These CPI−Ch complex coacervate phases were found to exhibit elastic behavior as evidenced by significantly higher elastic modulus (Gʹ) compared to viscous modulus (G ) in all the tested ratios and pH ranges. They also exhibited shear-thinning behavior during viscous flow. The complex coacervates formed at the optimum CPI-to-Ch ratio of 16:1 and pH of 6.0 demonstrated the highest Gʹ, G , and shear viscosity, which correlated well with the high strength of electrostatic interaction and thick-walled, sponge-like, less-porous microstructure at this condition. The higher shear viscosity of the coacervate at pH 6.0 was most likely induced by stronger attractive electrostatic interactions between CPI and Ch molecules, due to the formation of a rather densely packed complex coacervate structure. Hence, it can be concluded that the microstructural observations of denser structure correlated well with the rheological findings of stronger intermolecular bonds at the optimum CPI-to-Ch ratio of 16:1 and pH of 6.0. The complex coacervate phase formed at a CPI-to-Ch ratio of 16:1 and pH of 6.0 also showed glassy consistency at low temperatures and rubbery consistency above its glass-transition temperature. This study identified the potential for the newly developed CPI-Ch complex coacervate to be used as an encapsulating material due to its favorable strength. This would drastically reduce the wastage of byproducts, provide a solution to tackle the pressing global issue of wastage of byproducts, and bring about a more environmentally friendly paradigm.

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“…, 1989). Studies on complexes of ovalbumin (Noguchi, 1956), bovine serum albumin (Gurov & Nuss, 1986; Kato et al. , 1989; Dickinson & Galazka, 1992; Izgi & Dickinson, 1995; Dickinson & Pawlowsky, 1996; Galazka & Ledward, 1996) and dextran sulphate revealed that both electrostatic and covalent complexes were formed.…”

Section: Introductionmentioning

confidence: 99%

Electrosynthesis of κ‐carrageenan–ovalbumin complexes

Lii

Chen

et al. 2003

Int J of Food Sci Tech

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Electrosynthesis of kappa-carrageenan-ovalbumin complexes, in alkaline solution and containing both components in ratios varying from 1 : 5 to 5 : 1, is described. Complexes had compositions varying from 1 : 10 to 1 : 1.8. Components were covalently bound, as deduced from the insolubility of the complexes in 7 m urea, the infrared spectra, and thermogravimetric studies. The thermal stability of these complexes was higher than that of kappa-carrageenan and lower than that of ovalbumin

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Protein‐polysaccharide complexes as surfactants

Cited by 17 publications

References 2 publications

Mixed Layers of Sodium Caseinate + Dextran Sulfate: Influence of Order of Addition to Oil−Water Interface

Mixed Layers of Sodium Caseinate + Dextran Sulfate: Influence of Order of Addition to Oil−Water Interface

Rheological and Microstructural Characteristics of Canola Protein Isolate−Chitosan Complex Coacervates

Electrosynthesis of κ‐carrageenan–ovalbumin complexes

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