Interactions of Enzymes and a Lectin with a Chitin-Based Graft Copolymer Having Polysarcosine Side Chains

✍ Scribed by Rikiya Nakamura; Keigo Aoi; Masahiko Okada

• Publisher: John Wiley and Sons
• Year: 2004
• Tongue: English
• Weight: 108 KB
• Volume: 4
• Category: Article
• ISSN: 1616-5187
• DOI: 10.1002/mabi.200400008

✦ Synopsis

Abstract

Summary: 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 ^1^H 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 β‐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.

The structure of the graft copolymer, chitin‐graft‐polysarcosine 2, used here.

magnified imageThe structure of the graft copolymer, chitin‐graft‐polysarcosine 2, used here.