Interactions of enzymes and a lectin with a chitin-based graft copolymer having polysarcosine side chains.
Interactions of enzymes and a lectin with a chitin-based graft copolymer having polysarcosine side chains.
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DOI：
10.1002/mabi.200400008
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发表时间：
2004-06
影响因子：
4.6
通讯作者：
Rikiya Nakamura;K. Aoi;M. Okada
中科院分区：
文献类型：
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作者：
Rikiya Nakamura;K. Aoi;M. Okada
以几丁质酶、溶菌酶和麦胚凝集素（WGA）为底物，研究了水溶性几丁质衍生物几丁质接枝聚肌氨酸（2）的分子识别能力。采用几丁质酶和溶菌酶对2的降解性能进行了研究。与部分脱乙酰甲壳素（1）相比，对水具有较高亲和力的化合物2的分子量迅速下降。溶菌酶水解后得到的低分子量组分的1H NMR谱表明，几丁质骨架中的糖残基被溶菌酶特异性识别，然后骨架中的β-糖苷键被选择性水解。此外，通过酶联凝集素结合试验（ELLA）阐明了接枝共聚物2的几丁质主链对凝集素WGA的分子识别能力。结果表明，具有较低取代度（DS）值的接枝共聚物有效地与WGA相互作用。有趣的是，具有较长聚肌氨酸侧链的接枝共聚物比具有短侧链的接枝共聚物对WGA显示出更高的识别能力。
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.