EMULSIFYING PROPERTIES OF PROTEINS - EVALUATION OF A TURBIDIMETRIC TECHNIQUE
EMULSIFYING PROPERTIES OF PROTEINS - EVALUATION OF A TURBIDIMETRIC TECHNIQUE
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DOI:
10.1021/jf60217a041
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发表时间:
1978-01-01
影响因子:
6.1
通讯作者:
KINSELLA, JE
中科院分区:
文献类型:
--
作者:
PEARCE, KN;KINSELLA, JE
The capacity of protein to stabilize emulsions is related to the interfacial area that can be coated by the protein. According to the Mie theory for light scattering, a simple relationship exists between turbidity and the interfacial area of an emulsion. In this study, turbidimetry was evaluated as a method for measuring emulsifying properties of proteins. Emulsions were made by homogenizing known amounts of proteins and peanut oil. These emulsions were serially diluted to give absorbances of 0.01-0.6 at 500 nm. Several factors, i.e., degree of homogenization, type of homogenizer, protein concentration, volume of dispersion, oil volume fraction; pH and type of oil affected emulsion formation. The relative emulsifying activity of various food proteins (casein, .beta.-lactoglobulin, whey protein, yeast protein, ovalbumin and succinylated yeast proteins) was determined. Using a simple formula based on the turbidity, volume fraction of dispersed phase and weight of protein, an emulsifying activity index, related to the interfacial area of the emulsion, was calculated. Succinylated yeast proteins showed high emulsifying activities. This appeared to be related to the solubility of proteins and their resistance to surface denaturation.