Purification and Characterization of Alkane Solubilizing Factor Produced by Pseudomonas PG-1

概要

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The normal hexadecane emulsifying and solubilizing factor (PG-1 ESF C_<16>) produced by Pseudomonas PG-1 during growth on n-hexadecane was isolated and purified. The factor was composed of protein, carbohydrate and lipid, which were largely undialyzable. Ca^<2+> was necessary for activation and heat stability of the factor. Particle size of the factor was less than 10 nm. All the protein along with 68-74% of the carbohydrate in the factor was obtained in a single protein peak by gel filtration chromatography using Biogel P-30. The isolated protein fraction showed a 1-5 fold increase in n-hexadecane solubilizing activity. The isolated protein was shown to be a homogeneous, monomeric protein with a molecular weight of approximately 11,000 daltons by SDS-PAGE. The protein and carbohydrate moieties in the isolate were spearated by DEAE-cellulose chromatography. Neither purified protein nor carbohydrate showed n-hexadecane solubilizing activity separately, but when these were mixed full activity was restored. Hydrocarbon emulsifying activity was confined to the lipid fraction, which was isolated to the extent of 85% from the Biogel P-30 column by ethyl ether extraction.
社団法人日本生物工学会の論文
1990-06-25