Abstract

Emulsan, produced byAcinetobacter calcoaceticus RAG-1, consists of a lipoheteropolysaccharide-protein complex. The amount of protein in the complex depends on the purification procedure. Maximum hexadecane-in-water emulsifying activity of emulsan was obtained with preparations containing 8–16 % protein. Neither deproteinized preparations (apoemulsan) nor protein-rich preparations emulsified hexadecane-in-water; however, mixtures of these preparations (containing 10–15 % total protein) were potent emulsifiers. Emulsifying activity was also obtained with a mixture of apoemulsan and polysaccharide-free emulsan protein. The stimulatory role of protein in the activity of emulsan was also demonstrated by pronase treatment of the complex. The presence of protein in the complex was important for lowering interfacial tension between hexadecane and water. Apoemulsan solutions showedγ i values of 30 mN/m whereas, emulsan containing more than 6% protein showed values of 13–15 mN/m. Viscosity studies showed that: (i) The higher the protein content in the complex, the lower its intrinsic viscosity, indicating that association of protein with the polysaccharide backbone results in less extended conformation; (ii) the complex appears to be stable between 30 ° and 80 °C; and (iii) mixtures of apoemulsan and emulsan had intrinsic viscosities close to the value predicted from addition of the weight-fraction contribution of the individual components. The synergistic emulsifying activity of emulsan mixtures is explained in terms of surface tension lowering by the protein component and formation of stable interfacial films by the high molecular weight polysaccharide component.

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