Abstract
The mode of action of two chitinases from the Antarctic Arthrobacter sp. strain TAD20 on N-acetyl-chitooligomers and chitin polymers has been elucidated. Identification of the length of chitin oligomers following enzymatic hydrolysis was verified by using HPLC-based analysis. It was observed that the length of the oligomer is important for enzyme action. The enzymes cannot effectively hydrolyze chitin oligomers with a degree of polymerization lower than four. ArChiA is an endochitinase which hydrolyzes chitin substrates randomly, whereas ArChiB is an exochitinase which degrades chitin chains and N-acetyl-chitooligomers from the nonreducing end, releasing N-N′-diacetyl-chitobiose. ArChiB (100 μg/ml) inhibited spore germination and hyphal elongation of the phytopathogenic fungus Botrytis cinerea by 15% and 30%, respectively. A more pronounced effect was observed with ArChiA (100 μg/ml) resulting in 70% inhibition of spore germination and 60% inhibition of germ tube elongation. A slight additive effect was observed, when the two enzymes were used in combination, only on the inhibition of germ tube elongation.
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Acknowledgments
This work was supported by the CARAPAX "Quality of life and management of living resources" program QLKS-2000-00777. Research project funding by EC "FAIR 4140" and MIPAF "Risorse genetiche di organismi utili per il miglioramento di specie di interesse agrario e per un'agricoltura sostenibile" to M.L. is gratefully acknowledged. We thank Dr. N. Panopoulos for critical reading of the manuscript.
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Mavromatis, K., Lorito, M., Woo, S.L. et al. Mode of action and antifungal properties of two cold-adapted chitinases. Extremophiles 7, 385–390 (2003). https://doi.org/10.1007/s00792-003-0338-3
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DOI: https://doi.org/10.1007/s00792-003-0338-3