This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tsujibo, H.
Right arrow Articles by Inamori, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tsujibo, H.
Right arrow Articles by Inamori, Y.
Agricola
Right arrow Articles by Tsujibo, H.
Right arrow Articles by Inamori, Y.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, February 2003, p. 894-900, Vol. 69, No. 2
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.2.894-900.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Characterization of Chitinase Genes from an Alkaliphilic Actinomycete, Nocardiopsis prasina OPC-131

Hiroshi Tsujibo,* Takahiro Kubota, Mitsugu Yamamoto, Katsushiro Miyamoto, and Yoshihiko Inamori

Department of Microbiology, Osaka University of Pharmaceutical Sciences, Takatsuki, Osaka 569-1094, Japan

Received 8 July 2002/ Accepted 6 November 2002

An alkaliphilic actinomycete, Nocardiopsis prasina OPC-131, secretes chitinases, ChiA, ChiB, and ChiB{Delta}, in the presence of chitin. The genes encoding ChiA and ChiB were cloned and sequenced. The open reading frame (ORF) of chiA encoded a protein of 336 amino acids with a calculated molecular mass of 35,257 Da. ChiA consisted of only a catalytic domain and showed a significant homology with family 18 chitinases. The chiB ORF encoded a protein of 296 amino acids with a calculated molecular mass of 31,500 Da. ChiB is a modular enzyme consisting of a chitin-binding domain type 3 (ChtBD type 3) and a catalytic domain. The catalytic domain of ChiB showed significant similarity to Streptomyces family 19 chitinases. ChiB{Delta} was the truncated form of ChiB lacking ChtBD type 3. Expression plasmids coding for ChiA, ChiB, and ChiB{Delta} were constructed to investigate the biochemical properties of these recombinant proteins. These enzymes showed pHs and temperature optima similar to those of native enzymes. ChiB showed more efficient hydrolysis of chitin and stronger antifungal activity than ChiB{Delta}, indicating that the ChtBD type 3 of ChiB plays an important role in the efficient hydrolysis of chitin and in antifungal activity. Furthermore, the finding of family 19 chitinase in N. prasina OPC-131 suggests that family 19 chitinases are distributed widely in actinomycetes other than the genus Streptomyces.


* Corresponding author. Mailing address: Department of Microbiology, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan. Phone: (81-726) 90-1057. Fax: (81-726) 90-1057. E-mail: tsujibo{at}gly.oups.ac.jp.


Applied and Environmental Microbiology, February 2003, p. 894-900, Vol. 69, No. 2
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.2.894-900.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • LeCleir, G. R., Buchan, A., Hollibaugh, J. T. (2004). Chitinase Gene Sequences Retrieved from Diverse Aquatic Habitats Reveal Environment-Specific Distributions. Appl. Environ. Microbiol. 70: 6977-6983 [Abstract] [Full Text]  
  • Kawase, T., Saito, A., Sato, T., Kanai, R., Fujii, T., Nikaidou, N., Miyashita, K., Watanabe, T. (2004). Distribution and Phylogenetic Analysis of Family 19 Chitinases in Actinobacteria. Appl. Environ. Microbiol. 70: 1135-1144 [Abstract] [Full Text]