Soluble cell-bound and extracellular cyclodextrin glycosyltransferases of Bacillus macerans show identical enzymological characteristics and antigenicity

Noémi Nógrády, I. Pócsi, E. Katona, V. Jeney, Péter Boross, J. Tőzsér, József Fachet, A. Szentirmai

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5 Citations (Scopus)

Abstract

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

Original languageEnglish
Pages (from-to)335-340
Number of pages6
JournalJournal of Basic Microbiology
Volume36
Issue number5
Publication statusPublished - 1996

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Bacillus
Enzymes
Ion Exchange Chromatography
Protein Sorting Signals
Starch
Cell Wall
Adsorption
Gel Chromatography
Monoclonal Antibodies
Cell Membrane
cyclomaltodextrin glucanotransferase

ASJC Scopus subject areas

  • Genetics
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

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T1 - Soluble cell-bound and extracellular cyclodextrin glycosyltransferases of Bacillus macerans show identical enzymological characteristics and antigenicity

AU - Nógrády, Noémi

AU - Pócsi, I.

AU - Katona, E.

AU - Jeney, V.

AU - Boross, Péter

AU - Tőzsér, J.

AU - Fachet, József

AU - Szentirmai, A.

PY - 1996

Y1 - 1996

N2 - Soluble cell-bound and extracellular cyclodextrin glycosyltransferases of Bacillus macerans were purified to homogeneity using the subsequent steps of adsorption on starch, ion-exchange chromatography and gel filtration. The elution profiles and the relative molecular masses of the enzymes as well as their N-terminal sequences were found to be identical. Moreover, mouse monoclonal antibodies raised against the soluble cell-bound enzyme recognized equally well both the cell-bound and the extracellular enzyme preparations. Regarding that no signal peptide could be detected in either the cell-bound or the extracellular cyclodextrin glycosyltransferase the enzyme was probably entrapped between the cell membrane and the cell wall in the early stationary phase and was released during cell lysis without any modification.

AB - Soluble cell-bound and extracellular cyclodextrin glycosyltransferases of Bacillus macerans were purified to homogeneity using the subsequent steps of adsorption on starch, ion-exchange chromatography and gel filtration. The elution profiles and the relative molecular masses of the enzymes as well as their N-terminal sequences were found to be identical. Moreover, mouse monoclonal antibodies raised against the soluble cell-bound enzyme recognized equally well both the cell-bound and the extracellular enzyme preparations. Regarding that no signal peptide could be detected in either the cell-bound or the extracellular cyclodextrin glycosyltransferase the enzyme was probably entrapped between the cell membrane and the cell wall in the early stationary phase and was released during cell lysis without any modification.

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