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Gene cloning, nucleotide sequence and biochemical properties of a cytoplasmic cyclomaltodextrinase (neopullulanase) from Alicyclobacillus acidocaldarius, reclassification of a group of enzymes

  1. Jutta Matzke1,
  2. Anja Herrmann2,
  3. Erwin Schneider2,
  4. Evert P. Bakker1,*

Article first published online: 9 JAN 2006

DOI: 10.1111/j.1574-6968.2000.tb08933.x

Issue

FEMS Microbiology Letters

FEMS Microbiology Letters

Volume 183, Issue 1, pages 55–61, February 2000

Additional Information

How to Cite

Matzke, J., Herrmann, A., Schneider, E. and Bakker, E. P. (2000), Gene cloning, nucleotide sequence and biochemical properties of a cytoplasmic cyclomaltodextrinase (neopullulanase) from Alicyclobacillus acidocaldarius, reclassification of a group of enzymes. FEMS Microbiology Letters, 183: 55–61. doi: 10.1111/j.1574-6968.2000.tb08933.x

Author Information

  1. 1

    Abteilung Mikrobiologie, Universität Osnabrück, Barbarastaße 11, D-49069 Osnabrück, Germany

  2. 2

    Institut für Biologie, Abteilung Mikrobielle Bakterienphysiologie, Humboldt Universität zu Berlin, Chausséestraße 117, D-10115 Berlin, Germany

* *Corresponding author. Temporary address: Bioscience Center, University of Nagoya, Chikusa, Nagoya 464-01, Japan. Tel.: +81 (52) 7895202; Fax: +81 (52) 7895206, E-mail address: bakker@nuagr1.agr.nagoya-u.ac.jp

Publication History

  1. Issue published online: 9 JAN 2006
  2. Article first published online: 9 JAN 2006
  3. Received 23 September 1999, Revised 29 November 1999, Accepted 30 November 1999

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Keywords:

  • Neopullulanase;
  • Cyclomaltodextrinase;
  • Sub-cellular location;
  • α-Amylase family;
  • Amylopullulanase;
  • Alicyclobacillus acidocaldarius

Abstract

A gene encoding a cyclomaltodextrinase (neopullulanase) was cloned from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius ATCC27009 and its nucleotide sequence was determined. The encoded CdaA protein lacked an N-terminal signal sequence and aligned well with a family of bacterial proteins described as maltogenic α-amylases, neopullulanases or cyclomaltodextrinases. Escherichia coli cells harboring the cloned cdaA gene produced a 66-kDa protein that degraded pullulan in a sodium dodecyl sulfate-polyacrylamide gel. A. acidocaldarius cells grown on maltose, soluble starch or pullulan synthesized the same protein. Neopullulanase activity of the protein was cytoplasmic and its pH optimum of 5.5 was close to the pH value of the cytoplasm. CdaA degraded cyclomaltodextrins rapidly and pullulan (to panose) more slowly. It is proposed that CdaA functions as a cytoplasmic cyclomaltodextrinase (EC 3.2.1.54).

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