Related Experiment Video
Updated: Oct 2, 2026
Expression and Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein in Saccharomyces cerevisiae
Published on: March 10, 2012
Expression, purification, and characterization of a cobalt-activated chitin deacetylase (Cda2p) from Saccharomyces
Aggeliki Martinou1, Dimitris Koutsioulis, Vassilis Bouriotis
1Enzyme Biotechnology Division, Institute of Molecular Biology and Biotechnology, Vassilika Vouton 711 10, Heraklion, Crete, Greece.
Abstract:
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 approximately 43 kDa and a carbohydrate content of approximately 18% by weight. With glycol chitin as substrate, the optimum temperature for enzyme activity is 50 degrees C 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 COCl(2).
