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1

Chitosanase from Absidia orchidis

100%
Jaworska M. M., Kusaoke H.
Biotechnologia
|
2002
|
issue 2
200-206
EN
Absidia orchidis can be used as a source of several enzymes, amongst which chitosanase is one of the most interesting. Chitosanase hydrolyses the links between the mers of glucosamine or between mers of glucosamine and N-acetylglucosamine in the chains of chitosan and chitin. The aim of the presented work was the preliminary investigations of the chitosanase from the fungus Absidia orchidis. This chitosanase is an intracellular enzyme with molecular weight approx. 36 000 Da. The optimal conditions for a hydrolysis of chitosan were pH 4.5 and temperature 25C. This enzyme is stable at the optimal temperature for 24-48 hours, but after 7 days it was inactivated.
2

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

75%
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

75%
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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