Skip to main content
PMC home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1997 Feb;63(2):408–413. doi: 10.1128/aem.63.2.408-413.1997

Chitin Degradation Proteins Produced by the Marine Bacterium Vibrio harveyi Growing on Different Forms of Chitin

A L Svitil, S Chadhain, J A Moore, D L Kirchman
PMCID: PMC1389511  PMID: 16535505

Abstract

Relatively little is known about the number, diversity, and function of chitinases produced by bacteria, even though chitin is one of the most abundant polymers in nature. Because of the importance of chitin, especially in marine environments, we examined chitin-degrading proteins in the marine bacterium Vibrio harveyi. This bacterium had a higher growth rate and more chitinase activity when grown on (beta)-chitin (isolated from squid pen) than on (alpha)-chitin (isolated from snow crab), probably because of the more open structure of (beta)-chitin. When exposed to different types of chitin, V. harveyi excreted several chitin-degrading proteins into the culture media. Some chitinases were present with all of the tested chitins, while others were unique to a particular chitin. We cloned and identified six separate chitinase genes from V. harveyi. These chitinases appear to be unique based on DNA restriction patterns, immunological data, and enzyme activity. This marine bacterium and probably others appear to synthesize separate chitinases for efficient utilization of different forms of chitin and chitin by-products.

Full Text

The Full Text of this article is available as a PDF (948.2 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bassler B. L., Yu C., Lee Y. C., Roseman S. Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii. J Biol Chem. 1991 Dec 25;266(36):24276–24286. [PubMed] [Google Scholar]
  2. Fuchs R. L., McPherson S. A., Drahos D. J. Cloning of a Serratia marcescens Gene Encoding Chitinase. Appl Environ Microbiol. 1986 Mar;51(3):504–509. doi: 10.1128/aem.51.3.504-509.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Harpster M. H., Dunsmuir P. Nucleotide sequence of the chitinase B gene of Serratia marcescens QMB1466. Nucleic Acids Res. 1989 Jul 11;17(13):5395–5395. doi: 10.1093/nar/17.13.5395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hummel K. M., Penheiter A. R., Gathman A. C., Lilly W. W. Anomalous estimation of protease molecular weights using gelatin-containing Sds-Page. Anal Biochem. 1996 Jan 1;233(1):140–142. doi: 10.1006/abio.1996.0019. [DOI] [PubMed] [Google Scholar]
  5. Jannatipour M., Soto-Gil R. W., Childers L. C., Zyskind J. W. Translocation of Vibrio harveyi N,N'-diacetylchitobiase to the outer membrane of Escherichia coli. J Bacteriol. 1987 Aug;169(8):3785–3791. doi: 10.1128/jb.169.8.3785-3791.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Jones J. D., Grady K. L., Suslow T. V., Bedbrook J. R. Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J. 1986 Mar;5(3):467–473. doi: 10.1002/j.1460-2075.1986.tb04235.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Molano J., Durán A., Cabib E. A rapid and sensitive assay for chitinase using tritiated chitin. Anal Biochem. 1977 Dec;83(2):648–656. doi: 10.1016/0003-2697(77)90069-0. [DOI] [PubMed] [Google Scholar]
  8. Montgomery M. T., Kirchman D. L. Induction of Chitin-Binding Proteins during the Specific Attachment of the Marine Bacterium Vibrio harveyi to Chitin. Appl Environ Microbiol. 1994 Dec;60(12):4284–4288. doi: 10.1128/aem.60.12.4284-4288.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Montgomery M. T., Kirchman D. L. Role of Chitin-Binding Proteins in the Specific Attachment of the Marine Bacterium Vibrio harveyi to Chitin. Appl Environ Microbiol. 1993 Feb;59(2):373–379. doi: 10.1128/aem.59.2.373-379.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Radwan H. H., Plattner H. J., Menge U., Diekmann H. The 92-kDa chitinase from Streptomyces olivaceoviridis contains a lysine-C endoproteinase at its N-terminus. FEMS Microbiol Lett. 1994 Jul 1;120(1-2):31–35. doi: 10.1111/j.1574-6968.1994.tb07003.x. [DOI] [PubMed] [Google Scholar]
  11. Roberts R. L., Cabib E. Serratia marcescens chitinase: one-step purification and use for the determination of chitin. Anal Biochem. 1982 Dec;127(2):402–412. doi: 10.1016/0003-2697(82)90194-4. [DOI] [PubMed] [Google Scholar]
  12. Romaguera A., Menge U., Breves R., Diekmann H. Chitinases of Streptomyces olivaceoviridis and significance of processing for multiplicity. J Bacteriol. 1992 Jun;174(11):3450–3454. doi: 10.1128/jb.174.11.3450-3454.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Schnellmann J., Zeltins A., Blaak H., Schrempf H. The novel lectin-like protein CHB1 is encoded by a chitin-inducible Streptomyces olivaceoviridis gene and binds specifically to crystalline alpha-chitin of fungi and other organisms. Mol Microbiol. 1994 Sep;13(5):807–819. doi: 10.1111/j.1365-2958.1994.tb00473.x. [DOI] [PubMed] [Google Scholar]
  14. Sedgwick S. G., Nguyen T. M., Ellis J. M., Crowne H., Morris G. E. Rapid mapping by transposon mutagenesis of epitopes on the muscular dystrophy protein, dystrophin. Nucleic Acids Res. 1991 Nov 11;19(21):5889–5894. doi: 10.1093/nar/19.21.5889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Shigemasa Y., Saito K., Sashiwa H., Saimoto H. Enzymatic degradation of chitins and partially deacetylated chitins. Int J Biol Macromol. 1994 Feb;16(1):43–49. doi: 10.1016/0141-8130(94)90010-8. [DOI] [PubMed] [Google Scholar]
  16. Trudel J., Asselin A. Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal Biochem. 1989 May 1;178(2):362–366. doi: 10.1016/0003-2697(89)90653-2. [DOI] [PubMed] [Google Scholar]
  17. Tsujibo H., Orikoshi H., Tanno H., Fujimoto K., Miyamoto K., Imada C., Okami Y., Inamori Y. Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Altermonas sp. strain O-7. J Bacteriol. 1993 Jan;175(1):176–181. doi: 10.1128/jb.175.1.176-181.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Watanabe T., Oyanagi W., Suzuki K., Tanaka H. Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J Bacteriol. 1990 Jul;172(7):4017–4022. doi: 10.1128/jb.172.7.4017-4022.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES