title: A highly N-glycosylated chitin deacetylase derived from a novel strain of Mortierella sp. DY-52.
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.
authors: Glucosamine Saccharide Materials-National Research Laboratory (GSM-NRL), Division of Applied Bioscience and Biotechnology, Institute of Agricultural Science and Technology, Chonnam National University, Gwangju, Korea.
authors: Yong
authors: Y
authors: Zhao
authors: Gyung-Hyun
authors: GH
authors: Jo
authors: Wan-Taek
authors: WT
authors: Ju
authors: Woo-Jin
authors: WJ
authors: Jung
authors: Ro-Dong
authors: RD
authors: Park