Abstract
Chitinase (EC 3.2.1.14) was purified from the stomach of Japanese eel, Anguilla japonica, by fractionations with ammonium sulfate, Sephadex G-100 gel filtration, and DEAE-cellulose, CM-cellulose, and hydroxylapatite column chromatography. The molecular weight of this enzyme was 50,000 by SDS-PAGE, and the optimum pH was 4.4. The activity was strongly inhibited by Hg2+ and slightly activated by EDTA. The hydrolysis products of colloidal chitin by the enzyme were GlcNAc and GlcNAc2. When GlcNAc3–6 was used as substrate, GlcNAc and GlcNAc2 were recognized as final products with various ratios. GlcNAc2 was not hydrolyzed by this chitinase.
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