Comparison of Chitinase Isozymes from Yam Tuber—Enzymatic Factor Controlling the Lytic Activity of Chitinases
| Autor: | Yasuyuki Arakane, Daizo Koga, Hironori Hoshika, Chika Fujiya-Tsujimoto, Natsumi Kawashima, Yuji Sasaki |
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| Rok vydání: | 2000 |
| Předmět: |
Immunoblotting
Applied Microbiology and Biotechnology Biochemistry Isozyme Analytical Chemistry Microbiology chemistry.chemical_compound Fusarium Chitin Fusarium oxysporum Liliaceae Animals Molecular Biology Pathogenesis-related protein chemistry.chemical_classification biology Chitinases Organic Chemistry General Medicine Hydrogen-Ion Concentration Bombyx biology.organism_classification Elicitor Isoenzymes Kinetics Enzyme chemistry Lytic cycle Chitinase biology.protein Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 64:723-730 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.64.723 |
| Popis: | To evaluate the anti-pathogen activity of chitinases, we developed a new method for measuring the lytic activity, and investigated the correlation of the lytic activity with the enzymatic properties by using four chitinase isozymes, Chitinases E, F, H1 and G, which had been purified from yam tubers by column chromatography. Chitinases E, F and H1 had high lytic activity against the plant pathogen, Fusarium oxysporum, but Chitinase G did not. Chitinase E, which is the family 19 chitinase, was similar to Chitinases F and G in its antigenecity, but not to Chitinase H1 or H2. Chitinases H1 and H2 were recognized by the anti-Bombyx mori chitinase antibody, suggesting that Chitinases H1 and H2 are family 18 chitinases like B. mori chitinases. Chitinases E, F and H1 had two optimum pH ranges of 3-4 and 7.5-9 toward glycolchitin, but Chitinase G had only one optimum pH value of 5. Chitinases E, F and H1 had higher affinity to the polymer substrate, glycolchitin, than Chitinase G. These results suggest that the lytic activity of plant chitinases may be related to the chitin affinity and probably to the characteristic optimum pH value, or two values, but not related to its classification. The correlation of the lytic activity of a chitinase isozyme with its elicitor specificity is also discussed. |
| Databáze: | OpenAIRE |
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