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1

Purification and properties of chitin deacetylase from Absidia orchidis

100%
Szewczyk K. W., Orzeszak M.
Biotechnologia
|
2002
|
issue 2
48-59
EN
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.
2

The activity of chitin deacetylase and glycosidases of the crude enzyme extracts of Mucor rouxii mycelium

61%
Kolodziejska I., Wojtasz-Pajak A., Malesa-Ciecwierz M., Niecikowska C.
Biotechnologia
|
1997
|
issue 2
158-169
EN
The crude enzyme extract obtained from Mucor rouxii had optimal deacetylasde activity against chitosan acetylated in 39% in the Ph range of 5,2-5.9. Its activity against watger-soluble chitoologosaccharides, containing from 3 to 6 N-acetylglucosamine residues, was the higest in respect to (GlcNAc)s and nil against substrates containing less than 4 N-acetylglucosamine residues.Crystaline chitin was resistant to the deacetylase and to glycosidases present in the extract; amorphous chitin was noticeably more susceptible to these enzymes.Chitosan in the form of suspension was slightly deacetylated and hydrolysed by enzyme extracts.Solubilized chitosan acetylated in 39% was mostly susceptible to enzymatic deacetylation.The deacetylase activity in the extracts was inversely related and the chitonolytic activity was proportional to the deacetylation degree of soluble chitosan.
3

Enzymatic modification of chitin

61%
Kolodziejska I., Wojtasz-Pajak A., Sikorski Z. E.
Biotechnologia
|
1995
|
issue 3
133-139
EN
The role of chitinases, chitosanases, and chitin deacetylase in the biosynthesis and modification of chitin is presented.The biochemical properties of chitin deacetylase from Mucor rouxii are characterized in respect to its activity towards various chitin derivatives.This enzyme could be useful in biotechnological production of chitosan from chitin as an alternative method to tchermochemical deacetylation.
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