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Journal of Bacteriology, March 2001, p. 1773-1779, Vol. 183, No. 5
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.5.1773-1779.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Cloning, Sequences, and Characterization of Two Chitinase Genes from the Antarctic Arthrobacter sp. Strain TAD20: Isolation and Partial Characterization of the Enzymes

Thierry Lonhienne,1,2 Konstantinos Mavromatis,2 Constantin E. Vorgias,3 Laurent Buchon,4 Charles Gerday,1 and Vassilis Bouriotis2,*

Laboratory of Biochemistry, Institute of Chemistry B6, University of Liege, B-4000 Liege, Belgium1; Enzyme Technology Division, Institute of Molecular Biology and Biotechnology, and Department of Biology, Division of Applied Biology and Biotechnology, University of Crete, Heraklion, Crete, Greece2; National and Kapodistrian University of Athens, Faculty of Biology, Department of Biochemistry-Molecular Biology, Panepistimiopolis-Zographou, 15701 Athens, Greece3; and Laboratoire de Microbiologie du Froid, Institut Universitaire de Technologie, 27000 Evreux, France4

Received 14 August 2000/Accepted 6 December 2000

Arthrobacter sp. strain TAD20, a chitinolytic gram-positive organism, was isolated from the sea bottom along the Antarctic ice shell. Arthrobacter sp. strain TAD20 secretes two major chitinases, ChiA and ChiB (ArChiA and ArChiB), in response to chitin induction. A single chromosomal DNA fragment containing the genes coding for both chitinases was cloned in Escherichia coli. DNA sequencing analysis of this fragment revealed two contiguous open reading frames coding for the precursors of ArChiA (881 amino acids [aa]) and ArChiB (578 aa). ArChiA and ArChiB are modular enzymes consisting of a glycosyl-hydrolase family 18 catalytic domain as well as two and one chitin-binding domains, respectively. The catalytic domain of ArChiA exhibits 55% identity with a chitodextrinase from Vibrio furnissii. The ArChiB catalytic domain exhibits 33% identity with chitinase A of Bacillus circulans. The ArChiA chitin-binding domains are homologous to the chitin-binding domain of ArChiB. ArChiA and ArChiB were purified to homogeneity from the native Arthrobacter strain and partially characterized. Thermal unfolding of ArChiA, ArChiB, and chitinase A of Serratia marcescens was studied using differential scanning calorimetry. ArChiA and ArChiB, compared to their mesophilic counterpart, exhibited increased heat lability, similar to other cold-adapted enzymes.

* Corresponding author. Mailing address: Department of Biology, Division of Applied Biology and Biotechnology, University of Crete, P.O. Box 1470, Heraklion 71110, Crete, Greece. Phone: 30 81 394375. Fax: 30 81 394375. E-mail: bouriotis{at}imbb.forth.gr.

Journal of Bacteriology, March 2001, p. 1773-1779, Vol. 183, No. 5
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.5.1773-1779.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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