Part:BBa_K4424001
Chitinase used as fungicide and insecticide
Chitin, one of the most abundant naturally occurring polymers, is commonly found in fungal cell walls, exoskeletons of invertebrates, and insect gut linings. In insects, the chitin layer provides extra support and shields the soft tissue against mechanical damage and toxins. Throughout evolution, many organisms have acquired the ability to produce chitinolytic enzymes to digest chitin for nutrition. Since the catabolic reaction of chitin could be lethal for insect nymphs and larvae, chitinases have incredible potency in the development of biological insecticides [1][2][3] [4]. Besides, novel research has shown enhanced toxicity of insecticides, such as Bt toxins, when mixed with chitinase [5].
Several bacteria and fungi have been shown to produce hydrolytic enzymes after induction by the appropriate subtrates [5,6,7]. Mitchell and Alexander [8] have demonstrated biological control of Fusarium spp. and Pythium sp. by bacteria that degrade the cell wall of these plants pathogens. Mitchell and Hurwitz [9] protected tomato plants against damping off, caused by Pythium aphanidermatum (Edson) Fitzpatrick, by lytic Arthrobacter. Koths and Gunner [10] and Sneh [11] also demonstrated biological control of disease caused by Fusarium on carnation by using a chitinolytic Arthrobacter sp. Enterobacter cloaces (Jordon) Hormaeche and Edwards controlled Pythium in peas, sugar beet, and cucumber, probably by degrading the mycelium [12]. Campbell [13] and Campbell and Ephgrave [14] showed that hyphal lysis, induced by Bacillus sp. in soil was involved in a biological control of Gaeumannomyces graminis.
[1]Mahmood, S., Kumar, M., Kumari, P., Mahapatro, G. K., Banerjee, N., & Sarin, N. B. (2020). Novel insecticidal chitinase from the insect pathogen Xenorhabdus nematophila. International Journal of Biological Macromolecules. [2]Merzendorfer, H., & Zimoch, L. (2003). Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. Journal of Experimental Biology, 206(24), 4393-4412. [3]Patil, R. S., Ghormade, V., & Deshpande, M. V. (2000). Chitinolytic enzymes: an exploration. Enzyme and microbial technology, 26(7), 473-483. [4]Dahiya, N., Tewari, R., & Hoondal, G. S. (2006). Biotechnological aspects of chitinolytic enzymes: a review. Applied microbiology and biotechnology, 71(6), 773-782. [5]Bull, A. T. 1967 The enzime degradation of beta-glucan. Int. Biodeterior, Bull. 3:3-12. [6]Bull, A. T., and Chester, C. G. C. 1966. The biochemistry of laminarin and the nature of laminarinase. Adv. Enzymol. 28:325-364 [7]Ridout, C. J., Coley-Smith, J. R. and Lynch, J. M. 1986. Enzyme activity and electrophoretic profile of extracellular protein inducen in Trichoderma spp. by cell walls of rhizoctonia solani. J. Gen. Microbiol. 132:2345-2352 [8]Mitchell, R., & Alexander, M. 1961. The mycolytic phenomenon and biological control of Fusarium in soil. Nature, 190(4770), 109-110. [9]Mitchell, R., and Hurtwitz, R. 1965. Suppresion of pythium debaryanum by lytic rhizosphere bacteria. Phytopathology 55:156-158 [10]Koths, J. S. and Gunner, H. B. 1967. Establishment of a rhizosphere microflora on carnation as a means of plant protection in steamed greenhouse soil. Am. Soc. Hortic. Sci. 91:617-626 [11]Sneh, B. 1981. Use of rhizosphere chitinolytic bacteria for biological control of Fusarium Oxysporum f. sp. dianthi in carnation. Phytophatol. Z. 100:251-256 [12]Hadar, Y., Harman, G. E., Taylor, A. G., & Norton, J. M. (1983). Effects of pregermination of pea and cucumber seeds and of seed treatment with Enterobacter cloacae on rots caused by Pythium spp. Phytopathology, 73(9), 1322-1325. [13]Campbell, R. (1983). Ultrastructural studies of Gaeumannomyces graminis in the waterfilms on wheat roots and the effect of clay on the interaction between this fungus and antagonistic bacteria. Canadian Journal of Microbiology, 29(1), 39-45. [14]Campbell, R., & Ephgrave, J. M. (1983). Effect of bentonite clay on the growth of Gaeumannomyces graminis var. tritici and on its interactions with antagonistic bacteria. Microbiology, 129(3), 771-777. Sequence and Features
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