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  • Title: A highly N-glycosylated chitin deacetylase derived from a novel strain of Mortierella sp. DY-52.
    Author: Zhao Y, Jo GH, Ju WT, Jung WJ, Park RD.
    Journal: Biosci Biotechnol Biochem; 2011; 75(5):960-5. PubMed ID: 21597184.
    Abstract:
    Chitin deacetylase (CDA), the enzyme that catalyzes the hydrolysis of acetamido groups of GlcNAc in chitin, was purified from culture filtrate of the fungus Mortierella sp. DY-52 and characterized. The extracellular enzyme is likely to be a highly N-glycosylated protein with a pI of 4.2-4.8. Its apparent molecular weight was determined to be about 52 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and 67 kDa by size-exclusion chromatography. The enzyme had an optimum pH of 6.0 and an optimum temperature of 60 °C. Enzyme activity was slightly inhibited by 1-10 mM Co(2+) and strongly inhibited by 10 mM Cu(2+). It required at least two GlcNAc residues for catalysis. When (GlcNAc)(6) was used as substrate, K(m) and V(max) were determined to be 1.1 mM and 54.6 µmol min(-1) respectively.
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