PMID: 9443376Aug 1, 1997Paper

Purification and characterization of Bombyx mori chitinases

Insect Biochemistry and Molecular Biology
D KogaY Nagamatsu

Abstract

Two isozymes of chitinase (EC 3.2.1.14) were purified from the fifth-instar larvae of Bombyx mori by chromatography on DEAE-Cellulofine A-500, hydroxylapatite, Butyl-Toyopearl 650M, and Fractogel EMD DEAE 650 (M). These two isozymes were glycoproteins with different apparent molecular masses of 65 and 88 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pHs of the 65 and 88 kDa chitinases were 5.5 and 6.5, respectively, towards a short substrate, N-acetylchitopentaose (GlcNAc5), whereas their high activities were observed in a wide pH range between 4 and 10 towards a longer substrate, glycolchitin. Steady-state kinetic analysis of these chitinases was performed using a series of N-acetylchitooligosaccharides (GlcNAcn, n = 2-6) and glycolchitin as the substrates. Kinetic parameters for both chitinases could be obtained in the hydrolysis of glycolchitin, but not in that of N-acetylchitooligosaccharides because of strong substrate inhibition. Both chitinases similarly hydrolysed N-acetylchitooligosaccharides except for GlcNAc2 as follows: GlcNAc3 to GlcNAc plus GlcNAc2, GlcNAc4 to two molecules of GlcNAc2, GlcNAc5 to GlcNAc2 plus GlcNAc3, and GlcNAc6 to GlcNAc2 plus GlcNAc4 as w...Continue Reading

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