화학공학소재연구정보센터
Protein Expression and Purification, Vol.24, No.1, 111-116, 2002
Expression, purification, and characterization of a cobalt-activated chitin deacetylase (Cda2p) from Saccharomyces cerevisiae
Chitin deacetylase (Cda2p) (EC 3.5.1.41) from Saccharomyces cerevisiae has been purified from vegetative cells grown in galactose and further characterized. The enzyme is a glycoprotein with an apparent molecular mass of similar to43 kDa and a carbohydrate content of approximately 18% by weight. With glycol chitin as substrate, the optimum temperature for enzyme activity is 50degreesC and the pH optimum is 8.0. The enzyme requires at least two N-acetyl-D-glucosamine residues (chitobiose) for catalysis and is partially inhibited by acetate. Deglycosylation of the enzyme causes total loss of enzyme activity, which can be restored by the addition Of CoCl2. (C) 2002 Elsevier Science (USA).