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.
Nakamura
Rikiya
R
Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan.
Aoi
Keigo
K
Okada
Masahiko
M
D002686:Chitin / Q000737:chemistry / Q000378:metabolism*; D002688:Chitinases / Q000378:metabolism*; D009113:Muramidase / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011108:Polymers / Q000737:chemistry / Q000378:metabolism*; D012521:Sarcosine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity; D013997:Time Factors; D014909:Wheat Germ Agglutinins / Q000737:chemistry / Q000378:metabolism*
D010455:Peptides; D011108:Polymers; D014909:Wheat Germ Agglutinins; D002686:Chitin; C015475:polysarcosine; D002688:Chitinases; D009113:Muramidase; D012521:Sarcosine