Temperature-dependent complexation between sodium caseinate and gum arabic

Complex formation between sodium caseinate and gum arabic as a function of temperature was investigated using dynamic light scattering, fluorescence and NMR. At neutral pH, the turbidity and the particle size increased when sodium caseinate and gum arabic mixtures were heated in situ at temperatures...

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Bibliographic Details
Published in:Food hydrocolloids 2012, Vol.26 (1), p.82-88
Main Authors: Ye, Aiqian, Edwards, Patrick J.B., Gilliland, Janiene, Jameson, Geoffrey B., Singh, Harjinder
Format: Article
Language:English
Subjects:
Biological and medical sciences
Complexation
Dynamic tests
Dynamics
Fluorescence
Food additives
Food industries
Fundamental and applied biological sciences. Psychology
General aspects
Gum arabic
hydrophobic bonding
Hydrophobic interaction
light scattering
nuclear magnetic resonance spectroscopy
Particle size
Sodium
Sodium caseinate
Temperature
Turbidity
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Summary:Complex formation between sodium caseinate and gum arabic as a function of temperature was investigated using dynamic light scattering, fluorescence and NMR. At neutral pH, the turbidity and the particle size increased when sodium caseinate and gum arabic mixtures were heated in situ at temperatures above a critical temperature. The increases in turbidity and particle size were reversible. This effect was considered to be due to hydrophobic interactions, leading to the formation of a complex between sodium caseinate and gum arabic. 1H NMR spectroscopy showed that ANS, which bound to caseinate at low temperatures in caseinate solution or a caseinate–gum arabic mixture, was released at high temperatures upon formation of a caseinate or caseinate–gum arabic complex. This supported changes observed in the fluorescence of 8-anilino-1-naphthalene sulfonate upon binding to caseinate, which decreased at high temperatures for caseinate alone or when sodium caseinate was mixed with gum arabic. Light-scattering (turbidity) and dynamic light-scattering studies show that the temperature-dependent complexation between sodium caseinate and gum arabic was sensitive to the mass ratio of protein to gum arabic (greater complexation at a 1:5 ratio than a 1:1 ratio) and the pH (maximum complexation at pH 6.5). [Display omitted]
ISSN:0268-005X
1873-7137
DOI:10.1016/j.foodhyd.2011.04.004