Emulsifying properties of ovalbumin in mixtures with sulphated polysaccharides: effects of pH, ionic strength, heat and high-pressure treatment

Galazka, Vanda B.; Dickinson, Eric; Ledward, D.A.

doi:10.1002/1097-0010(200006)80:8<1219::aid-jsfa626>3.0.co;2-w

Cited by 64 publications

(14 citation statements)

References 35 publications

(42 reference statements)

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“…The less acidic microenvironments (i.e., CPTEH:CPH) improved Ova stability than at acidic pH, where stronger complexation can result in protein aggregation [31,44]. On the other hand, precipitation of albumin is expected when the pH of the aqueous environment approaches the isoelectric point ($4.8).…”

Section: Discussionmentioning

confidence: 99%

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Amphiphilic polyanhydrides for protein stabilization and release

et al. 2007

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The overall goal of this research is to design novel amphiphilic biodegradable systems based on polyanhydrides for the stabilization and sustained release of peptides and proteins. Accordingly, copolymers of the anhydrides, 1,6-bis(p-carboxyphenoxy)hexane (CPH) and 1,8-bis(p-carboxyphenoxy)-3,6-dioxaoctane (CPTEG), which are monomer-containing oligomeric ethylene glycol moieties, have been synthesized. Microspheres of different CPTEG:CPH compositions have been fabricated by two non-aqueous methods: solid/oil/oil double emulsion and cryogenic atomization. The ability of this amphiphilic polymeric system to stabilize model proteins (i.e., lysozyme and ovalbumin) was investigated. The structure of both the encapsulated as well as the released protein was monitored using gel electrophoresis, circular dichroism, and fluorescence spectroscopy. It was found that the CPTEG:CPH system preserves the structural hierarchy of the encapsulated proteins. Activity studies of the released protein indicate the CPTEG:CPH system retains the biological activity of the released protein. These results are promising for future in vivo studies, which involve the design of novel biodegradable polyanhydride carriers for the stabilization and sustained release of therapeutic peptides and proteins. r

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Section: Discussionmentioning

confidence: 99%

“…On the other hand, Ova has been well studied as a model antigen and is composed of 385 residues (48 kDa). It has a molten globular or intermediate unstable state in acidic surroundings, which is deleterious for its activity [31]. Two nonaqueous methods, S/O/O and CA, were used to fabricate the microspheres.…”

Section: Introductionmentioning

confidence: 99%

Amphiphilic polyanhydrides for protein stabilization and release

et al. 2007

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“…This finding is consistent with droplet size and zeta-potential results and suggests that the interaction in protein-stabilized emulsion can be principally attributed to electrostatic force. The addition of salt decreases the emulsifying activities similar to the one found in ovalbumin (Galazka et al, 2000), whey protein isolate (Pearce and Kinsella, 1978), and even albumin-dextran sulfate stabilized emulsions (Kato et al, 1989). The ESI indices of emulsions which were stable even after 48 h were shown in Table 4.…”

Section: Effect On Emulsions Stabilitymentioning

confidence: 99%

Ability of flaxseed and soybean protein concentrates to stabilize oil-in-water emulsions

Wang

Liu

Wang

et al. 2010

Journal of Food Engineering

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“…Lower pressures, from 50 to 200 MPa were used to treat emulsions prepared with a plant protein from broad bean and reported a slight increase in average droplet size (d 43 ) (Galazka, Dickinson, & Ledward, 1999). Emulsions prepared with ovalbumin showed a major change in average droplet size (d 43 ) when exposed to high-pressure treatments above 400 MPa (Galazka, Dickinson, & Ledward, 2000).…”

Section: Treatment Of Emulsions At Pasteurisation Conditionsmentioning

confidence: 99%