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Chitin oligosaccharides are known to be common elicitors of plant defense responses and to induce the chitinase production to protect plants from fungal infection and insect attack. 6,11–13 )Ĭhitin is not a component of plant cell walls but is the major component of fungal cell walls. 10 ) Some chitinases are multi-modular in structure, composed of more than one functional domain, such as a catalytic domain and a carbohydrate binding module (CBM) to bind and assist in long chitin chain degradation. 7,8 ) The GH-18 chitinases have a triosephosphate isomerase (TIM-barrel) fold as a catalytic domain and have a retaining mechanism, 9 ) while the GH-19 chitinases are comprised of lysozyme-like (α + β)-folds and use an inverting mechanism. 6 ) The bacterial chitinases of family GH-18 are classified into three subfamilies: A, B, and C. net retention or inversion of the anomeric configuration of the reaction product. 5 ) The members of the two families differ in primary sequence, three dimensional structure, and stereospecific catalytic mechanisms, i.e. Various chitinases and their genes from bacteria to eukaryotes have been investigated 2 ) and have been mainly classified into two glycoside hydrolase families, GH-18 and GH-19, based on amino acid sequence similarities ( ). 3,4 ) Chitinases hydrolyze chitin by cleaving the glycosidic bond and produce oligo-, di-, or monosaccharides. 1,2 ) It is a linear insoluble homopolysaccharide composed of N-acetyl-D-glucosamine (GlcNAc) residues linked by β-1,4-glycosidic bonds that is relatively resistant to degradation due to its rigid structure. Based on amino acid sequence similarities and site-directed mutagenesis, Glu691 and Glu1177 in the two GH-18 domains were identified as catalytic residues.Ĭhitin, a common constituent of the shells of crustaceans, the cuticles of invertebrates, and fungal cell walls, is the second most abundant biomass next to plant cellulose in nature. Various insoluble chitins were hydrolyzed to N, N’-diacetyl-D-chitobiose as the final product. Its biochemical properties were also characterized. The vacuum-ultraviolet circular dichroism spectrum of the enzyme strongly suggested the presence of a β-stranded-rich structure in the N-terminus. The two catalytic domains at the C-terminal region were classified as typical glycoside hydrolase family 18 chitinases, whereas the N-terminal region showed no sequence similarity to other known proteins. Here, we report that active ChiW lacking the anchoring domains in the N-terminus was successfully overproduced in Escherichia coli and purified to homogeneity.

FPU-7 chitinases, ChiW, a novel monomeric chitinase with a molecular mass of 150 kDa, is expressed as a cell surface molecule. strain FPU-7 produces several different chitinases and effectively hydrolyzes robust chitin.

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