Purification and properties of chitin deacetylase from Absidia orchidis
Languages of publication
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.
Publication order reference
K. W. Szewczyk, Wydzial Inzynierii Chemicznej i Procesowej, Politechnika Warszawska, ul. Warynskiego 1, 00-645 Warszawa, Poland