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A bacterium isolated from activated sludge formed a visible floc and also produced an exoenzyme that could bring about deflocculation. Scanning electron microscopic examination revealed that the cells were embedded in a film mesh in the floc, which disappeared after treatment with the deflocculating enzyme. Polysaccharides isolated from the floc were fractionated into three fractions by diethylaminoethyl-Sephadex A-25 column chromatography, whereas those from the free cells were fractionated into only two fractions. The missing fraction was a mucopolysaccharide composed of glucosamine, glucose, mannose, galactose, and rhamnose and was hydrolyzed to oligosaccharides by the deflocculating enzyme. The other two fractions were resistant to the enzyme. These results show that the mesh structure of the floc is dependent on a mucopolysaccharide hydrolyzed by the deflocculating enzyme.

Exocellular mucopolysaccharide closely related to bacterial floc formation