SOLUBLE CELL-BOUND AND EXTRACELLULAR CYCLODEXTRIN GLYCOSYLTRANSFERASES OF BACILLUS-MACERANS SHOW IDENTICAL ENZYMOLOGICAL CHARACTERISTICS AND ANTIGENICITY

Soluble cell-bound and extracellular cyclodextrin glycosyltransferases of Bacillus macerans were purified to homogeneity using the subsequen t steps of adsorption on starch, ion-exchange chromatography and gel f iltration. The elution profiles and the relative molecular masses of t he enzymes as well as their N-terminal sequences were found to be iden tical. Moreover, mouse monoclonal antibodies raised against the solubl e cell-bound enzyme recognised equally well both the cell-bound and th e extracellular enzyme preparations. Regarding that no signal peptide could be detected in either the cell-bound or the extracellular cyclod extrin glycosyltransferase the enzyme was probably entrapped between t he cell membrane and the cell wall in the early stationary phase and w as released during cell lysis without any modification.