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Competitive binding of highly de-N-acetylated chitosans and N,N′-diacetylchitobiose to lysozyme from chicken egg white studied by 1H NMR spectroscopy by Are Kristiansen; Kjell M. Vårum; Hans Grasdalen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Chitosan is a linear polysaccharide which contains 2-acetamido-2-deoxy-/3-o-glucose (GlcNAc; A-unit) and 2-amino-2-deoxy-/3-D-glucose (GIcN; D-unit) residues linked through (1 ~ 4) glycosidic linkages. It has previously been shown that A-units and D-units are randomly distributed along the polymer chain in water-soluble, partially N-acetylated chitosans prepared by homogeneous or heterogeneous deacetylation of chitin [1,2]. Thus, the neighbourhood of units (e.g. the fractions of diads and triads) in the polymer is determined only by the fraction of acetylated units, F A (FAA = F~: FAD ~ FDA = FA \* FD; FDD = FD 2; FAAA = ~2 etc.). Lysozyme hydrolyses /3-(1 ~ 4) linkages in chitin. Berger and Weiser [3] showed that fully de-N-acetylated chitosan (F A = 0) is not degraded by lysozyme. Nordtveit et al. [4] reported that the initial degradation rate (by lysozyme from chicken egg white) of partially N-acetylated chitosans increases in proportion to F A to the power of 3.6, and that the degradation rate is negligible at low fractions of acetylated units (F A < 0.04). Lysozyme contains six binding subsites normally designated by the letters A-F, with cleavage occurring between sugar resid

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Author

Are Kristiansen; Kjell M. Vårum; Hans Grasdalen

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0008-6215)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)