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| Web URL(s): | http://apsjournals.apsnet.org/doi/pdf/10.1094/PHYTO.2001.91.2.204
Last checked: 02/17/2010
Requires: PDF Reader |
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| Publication Type:
| Refereed |
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| Author(s): | Zhang, Z.;
Yuen, G. Y.;
Sarath, G.;
Penheiter, A. R. |
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| Author Affiliation: | Zhang and Yuen: Department of Plant Pathology, University of Nebraska, Lincoln, NE; Sarath and Penheiter: Department of Biochemistry, University of Nebraska, Lincoln, NE |
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| Title: | Chitinases from the plant disease biocontrol agent, Stenotrophomonas maltophilia C3 |
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| Section: | Biological control
Other records with the "Biological control" Section
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| Source: | Phytopathology. Vol. 91, No. 2, February 2001, p. 204-211. |
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| Publishing Information: | St. Paul, MN: American Phytopathological Society |
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| # of Pages: | 8 |
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| Related Web URL: | http://apsjournals.apsnet.org/doi/abs/10.1094/PHYTO.2001.91.2.204
Last checked: 02/17/2010
Notes: Abstract only |
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| Keywords: | TIC Keywords: Environmental factors; Enzyme activity; Amino acids; Chitinase; Stenotrophomonas maltophilia; Biological control; Bipolaris sorokiniana; Disease control; Ammonium sulfate; Precipitation; Chromatography; Proteins; Enzymes; Inhibitors
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| Abstract/Contents: | "Stenotrophomonas maltophilia strain C3, a biocontrol agent of Bipolaris sorokiniana in turfgrass, produced chitinases in broth media containing chitin. Chitinases were partially purified from culture fluid by ammonium sulfate precipitation and chitin affinity chromatography. The chromatography fraction with the highest specific chitinase activity was inhibitory to conidial germination and germ-tube elongation of B. sorokiniana, but it was less inhibitory than the protein fraction or the raw culture filtrate. The fraction exhibited strong exochitinase and weak endochitinase activity. Optimum temperature and pH for chitinase activity were 45 to 50°C and 4.5 to 5.0, respectively. Chitinase activity was inhibited by Hg2+ and Fe3+, but not by other metal ions or enzyme inhibitors. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the chromatography fraction revealed the presence of five protein bands of 25, 32, 48, 65, and 75 kDa. Partial amino acid sequences of the 32-, 65-, and 75-kDa proteins indicated that they are homologous to known bacterial chitinases. There was no homology found in the partial amino acid sequences of the 25- and 48-kDa proteins to any known chitinases. Five chitinase-active proteins were detected in the protein and chromatography fractions by activity gels, but when each protein was extracted and re-electrophoresed separately under denaturing conditions, only 32- or 48-kDa proteins were revealed. It was concluded that strain C3 produces at least two chitinases that are antifungal." |
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| Language: | English |
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| References: | 38 |
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| Note: | Figures
Tables
Graphs |
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| ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Zhang, Z., G. Y. Yuen, G. Sarath, and A. R. Penheiter. 2001. Chitinases from the plant disease biocontrol agent, Stenotrophomonas maltophilia C3. Phytopathology. 91(2):p. 204-211. |
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| Web URL(s):
http://apsjournals.apsnet.org/doi/pdf/10.1094/PHYTO.2001.91.2.204
Last checked: 02/17/2010
Requires: PDF Reader |
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MSU catalog number: SB 599 .P48 |
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