2004年6月
Interactions of enzymes and a lectin with a chitin-based graft copolymer having polysarcosine side chains
MACROMOLECULAR BIOSCIENCE
- ,
- ,
- 巻
- 4
- 号
- 6
- 開始ページ
- 610
- 終了ページ
- 615
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1002/mabi.200400008
- 出版者・発行元
- WILEY-V C H VERLAG GMBH
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 deactylated chitin (1). The H-1 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 of graft copolymer 2 toward the lectin WGA was elucidated by the enyzme-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 poly-sarcosine side chains showed higher recognition ability toward WGA than that having short side chains.
- リンク情報
- ID情報
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- DOI : 10.1002/mabi.200400008
- ISSN : 1616-5187
- Web of Science ID : WOS:000222440100009