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Abstrakt

Chitin deacetylase is the only known enzyme which is able to deacetylate N-acetyl-D-glucosamine units in chitin or chitosan chains. As chitin can hardly be dissolved in organic/inorganic solvents, new solvents are still searched. Ionic liquids are promising for that application and for homophase enzymatic deacetylation. The aim of the work was to investigate the influence of selected ionic liquids on activity of chitin deacetylase.

It has been shown that [Amim] ionic liquids increase the activity of chitin deacetylase. The highest activity was observed for [Amim][Cl]. Ionic liquids with shorter (ethyl (C2)) and longer side chain (buthyl (C4)) only insignificantly influenced the activity of the enzyme. All tested ionic liquids with [Br] anion increased the activity of chitin deacetylase while the [Emim] and [Bmim] cation in combination with [Cl] anion inhibited the activity of the enzyme.

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Autorzy i Afiliacje

Izabela Aspras
Małgorzata Kamińska
Kamil Karzyński
Mateusz Kawka
Małgorzata M. Jaworska

Abstrakt

The possibility of producing chitosan by enzymatic deacetylation of chitin has been the subject of numerous investigations over the last twenty years, but to date no satisfactory method has been developed. In this paper the influence of chitin chain conformation and chitin particle crystallinity on the enzymatic deacetylation of chitin is investigated to determine the relative importance of these two factors on the process. It is shown that the high crystallinity of chitin is the main obstacle to converting chitin to chitosan by enzymatic deacetylation.

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Autorzy i Afiliacje

Małgorzata M. Jaworska
George A.F. Roberts

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