Interactions of enzymes and a lectin with a chitin-based graft copolymer having polysarcosine side chains.

The molecular-recognition abilities of a water-soluble chitin derivative, chitin-graft-polysarcosine (2) were investigated using chitinase, lysozyme, and wheat germ agglutinin (WGA). The enzymatic degradabilities of 2 were evaluated using chitinase and lysozyme. The molecular weight of those compounds of 2 with a higher affinity toward water decreased rapidly, as compared with partially deacetylated chitin (1). The 1H NMR spectrum of the low-molecular-weight fraction, yielded after lysozymic hydrolysis, indicated that saccharide residues in the chitinous backbone were specifically recognized by the lysozyme, then beta-glycosidic linkages in the backbone were selectively hydrolyzed. Furthermore, the molecular-recognition ability of the chitinous backbone of graft copolymer 2 toward the lectin WGA was elucidated by the enzyme-linked lectin-binding assay (ELLA). It was revealed that the graft copolymer with a lower degree of substitution (DS) value efficiently interacted with WGA. Interestingly, a graft copolymer having longer polysarcosine side chains showed higher recognition ability toward WGA than that having short side chains.