The mode of action of chitin deacetylase from the fungus Mucor rouxii on N-
acetylchitooligosaccharides with a degree of polymerization 1-7 has been el
ucidated.
identification of the sequence of chitin oligomers following enzymatic deac
etylation was verified by the alternative use of two specific exo-glycosida
ses in conjunction with HPLC. The results were further verified by H-1-NMR
spectroscopy.
It was observed that the length of the oligomer is important for enzyme act
ion. The enzyme cannot effectively deacetylate chitin oligomers with a degr
ee of polymerization lower than three. Tetra-N-acetylchitotetraose and pent
a-N-acetylchitopentaose an fully deacetylated by the enzyme, while in the c
ase of tri-N-acetylchitutriose, hexa-N-acetylchitohexaose and hepta-N-acety
lchitoheptaose the reducing-end residue always remains intact. Furthermore,
the enzyme initially removes an acetyl group from the nonreducing-end resi
due of all chitin oligomers with a degree of polymerization higher than 2,
and further catalyses the hydrolysis of the following acetamido groups in a
processive fashion.
The results are in agreement with the mode of action that the same enzyme e
xhibits on partially deacetylated water soluble chitosan polymers.