Methods of purification of chitin deacetylase are discussed. A two step method of purification of chitin deacetylase from mycelial extracts of the fungus Absidia orchidis by chromatography is presented. The crude enzyme extract was purified by a gel chromatography and then by ion exchange chromatography. Specific activity of purified enzyme was 12.3 U/mg and final purification degree was 147. The apparent molecular mass of the enzyme was 75 kDa. When O ? hydroxyethylated chitin (glycol chitin) was used as a substrate, the optimum pH for enzyme activity was 5,5 and the optimum temperature was 50?C.
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