Levansucrase of Bacillus subtilis

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Abstract
A macromolecular complex including an inactive and protease‐sensitive form of levansucrase was isolated from phenol treatment of Bacillus subtilis. This complex has a weak affinity for hydroxyapatite. Its molecular weight is evaluated at 300000. This levansucrase form may be activated either by Triton X‐100, above its critical micellar concentration, or by phospholipase C. The enzyme form associated with the complex is quite different from the exocellular levansucrase, which is protease‐insensitive and detergent‐insensitive, shows high affinity for hydroxyapatite and has a molecular weight of 54000. Triton X‐100 disaggregates this complex. The active levansucrase released becomes protease‐insensitive and has the same apparent sedimentation coefficient as the exocellular enzyme. Possible relationships between the existence of this trapped complex and the secretion process of levansucrase are discussed.