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자료유형
학술저널
저자정보
저널정보
한국식품영양과학회 Journal of Food Science and Nutrition Journal of Food Science and Nutrition Vol.3 No.2
발행연도
1998.6
수록면
143 - 151 (9page)

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Protein-surfactant interactions have been investigated by measuring ξ-potential of β-lactoglobulin-coated emulsion droplets and β-lactoglobulin in solution in the presence of surfactant, with particular emphasis on the effect of protein heat treatment (70℃, 30 min). When ionic surfactant (SDS or DATEM) is added to the protein solution, the ξ-potential of the mixture is found to increase with increasing surfactant concentration, indicating surfactant binding to the protein molecules. For heat-denatured protein, it has been observed that the ξ-potential tends to be lower than that of the native protein. The effect of surfactant on emulsions is rather complicated. With SDS, small amounts of surfactant addition induce a sharp increase in zeta potential arising from the specific interaction of surfactant with protein. With further surfactant addition, there is a gradual reduction in the ξ-potential, presumably caused by the displacement of adsorbed protein (and protein-surfactant complex) from the emulsion droplet surface by the excess of SDS molecules. At even higher surfactant concentrations, the measured zeta potential appears to increase slightly, possibly due to the formation of a surfactant micellar structure at the oil droplet surface. This behaviour contrasts with the results of the corresponding systems containing the anionic emulsifier DATEM, in which the ξ-potential of the system is found to increase continuously with R, particularly at very low surfactant concentration. Overall, such behaviour is consistent with a combination of complexation and competitive displacement between surfactant and protein occurring at the oil-water interface. In addition, it has also been found that above the CMC, there is a time-dependent increase in the negative ξ-potential of emulsion droplets in solutions of SDS, possibly due to the solublization of oil droplets into surfactant micelles in the aqueous bulk phase.

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Abstract

INTRODUCTION

MATERIALS AND METHODS

RESULTS AND DISCUSSION

CONCLUSIONS

REFERENCES

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