Protein-stabilized emulsions: effects of modification on the emulsifying activity of bovine serum albumin in a model system

Waniska, Ralph D.; Shetty, Jayarama K.; Kinsella, John E.

doi:10.1021/jf00106a037

Cited by 64 publications

(64 citation statements)

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“…The ability of discrete emulsion droplets to remain dispersed without creaming, flocculating, coalescing, or oiling off is defined as emulsifying stability (Waniska, Shetty, & Kinsella, 1981). The emulsifying stability index (ESI) values of SPI emulsions are illustrated in Fig.…”

Section: Resultsmentioning

confidence: 99%

Effects of different oils on the properties of soy protein isolate emulsions and gels

Campbell

Euston

2009

Food Research International

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Section: Resultsmentioning

confidence: 99%

Effects of different oils on the properties of soy protein isolate emulsions and gels

Campbell

Euston

2009

Food Research International

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“…The oil droplet size distribution in the emulsion was assessed with the statistical diameter according to FERET using a light microscope at 600 x magnification WEB Carl Zeiss, Jena, GDR); for this purpose the emulsion is diluted 1 : lo00 with 0.05 % aqueous sodium dodecyl sulphate solution [6].…”

Section: Methodsmentioning

confidence: 99%

Tension of oil‐water interface and properties of O/W emulsions in dependence of faba bean globulins

Schmandke

Schultz

Schmidt

et al. 1990

Nahrung

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Compared with faba bean globulin the improved flow, gelifying, surface and emulsifying properties of aqueous solution of the corresponding acetylated derivatives are reflected in O/W emulsions by their enhanced stability.Investigations were made concerning the changes of the flow, gelifying [l], surface [2] and emulsifying [2,3] behaviour of aqueous faba bean globulin solutions dependent on their acetylation degree and the rheological properties of O/W emulsions stabilized by acetylated faba bean globulins [4]. The aim of the present paper is to extend our knowledge with regard to the time-dependent interfacial tension of oil-water interface for absorption from faba bean globulin solutions and to the long-term stability of corresponding Om-emulsions. Materials and methodsFaba bean globulin was used, prepared from faba bean flour by extraction at pH 7.5. Acetylation (degree -97 %) occurred during the extraction after adding acetic anhydride [5].Commercial and purified sunflower oil was used as the oil phase. For purification the sunflower oil was mixed 1 : 2 with aluminum oxide (standardized according to BROCKMANN) and shaken for 30 min at room temperature; fitration was repeated twice through a paper (Nr. 238 ; VEB Spaialpapierfabrik Niederschlag, GDR) filter. The so treated oil contained: free fatty acids 0.01 %; carbonyls 13 mg hexana1/100 g; peroxides 2 ml 0.002 N Na,S,O,/g; phosphatides non-detectable.The interfacial tension between aqueous protein solution and oil was measured by the ring method of DU Nouv using a tensiometer (Fa. Kriiss, Hamburg, FRG).O/W emulsions were prepared by dissolving protein in bidistilled water containing 0.02 % NaN, as preservative and stirred continously with a magnetic stirrer for 2 h. The solution obtained was centrifugated at 15,000 x g for 30 min; the content of protein was determined and the solution diluted to the required concentration.Sunflower oil was added slowly to the aqueous phase and dispersed with a magnetic stirrer. This coarse emulsion was then homogenized by an ultrasonic disintegrator USD-20 (Academy of Sciences of the GDR VDE Berlin-Buch) under the following conditions : temperature 50 "C, power 400 W/cm', sonification time 3 times each for 1 min in 3 min intervals. The pH of the homogenized emulsions was 6.5 and was adjusted with 0.5 N NaOH or 2 N HCI with the aid of a special blade stirrer. The emulsions were stored at +4 -6 "C for 24 h before evaluating apparent viscosity and oil droplet size distribution.The apparent viscosity of the emulsions was determined at 25 "C by means of the rotating viscosimeter Rheotest 2 (VEB MLW Medingen, GDR), a coaxial cylinder system with a gap of 1 mm (measuring system s 1).The oil droplet size distribution in the emulsion was assessed with the statistical diameter according to FERET using a light microscope at 600 x magnification WEB Carl Zeiss, Jena, GDR); for this purpose the emulsion is diluted 1 : lo00 with 0.05 % aqueous sodium dodecyl sulphate solution [6]. 25'

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“…4), suggesting that the disulfide bonds play an important role in stabilizing the emulsion as well as the protein molecular weight. Waniska, Shetty, and Kinsella (1981) also reported that a reduction in disulfide bonds reduced the emulsifying activities (EA) of bovine serum albumin. When the sulphydryl groups in the proteins were chemically blocked, the emulsions that formed were less stable (Wu et al, 2011).…”

Section: Sds-pagementioning

confidence: 99%

Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

Zhang

2015

Food Hydrocolloids

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Protein-stabilized emulsions: effects of modification on the emulsifying activity of bovine serum albumin in a model system

Cited by 64 publications

References 13 publications

Effects of different oils on the properties of soy protein isolate emulsions and gels

Effects of different oils on the properties of soy protein isolate emulsions and gels

Tension of oil‐water interface and properties of O/W emulsions in dependence of faba bean globulins

Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

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