Heterogeneous components of chitosans.
The main objectives of the research were to compare the components of partially N-deacetylated chitins prepared identically from native chitin and a chitin regenerated from a heavily deacetylated chitosan. Additionally, to determine if any of the water-soluble components would serve as substrates in a study of a Chitinase isolated from soy bean hull. The brief heating of suspended chitins in 20% (w/w) NaOH resulted in similar degrees of N-deacetylation, the native chitin giving DAc 0.84 and the regenerated chitin DAc 0.79-0.72, with DAc indicating the proportion of glucosamine residues that are acetylated. Evidence for the nature of the hydrolysis of acetamido groups was provided by analyses of the water-soluble and -insoluble Smith degradation products. The water-soluble fraction derived from the native chitin comprised very small amounts of erythrityl N-acetyl glucosaminoside (GlcNAc1E), erythrityl N,N'-diacetyl chitobioside (GlcNAc2E), and erythrityl N,N',N''-triacetyl chitotrioside (GlcNAc3E), each identified by MALDI-TOF mass spectrometry of the butanoyl derivative. The water-insoluble products, as analyzed by light scattering detection method of their butanoyl esters and corrected for their composition, had a molecular weight (Mw) of 25 kDa, corresponding to about 120 N-acetyl glucosaminyl repeating residues (DPw), contrasting to that of 140 kDa with DPw of 680 for the parent chitin. Much of the decrease in the molecular weight of the polymer occurs by the loss of sugar residues by alkaline peeling at reducing terminals. For the regenerated chitin (DAc 1.0), prepared by N-reacetylation of a commercial chitosan (DAc 0.15), the resulting Smith products comprised erythritol and a series of N-acetyl glucosaminyl erythritol homologues of up to at least 39 N-acetyl glucosaminyl repeating residues, reflecting greater heterogeneity in the hydrolysis of acetamido groups along the polymer chain than what was seen for the native chitin. Of the water-soluble Smith products, GlcNAc5-7E were good substrates for chitinase isolated from soybean hull.
Yang
Byung Y
BY
Department of Biochemistry, College of Medicine, The University of Iowa, Iowa City, Iowa 52242, United States.
Ding
Qiong
Q
Montgomery
Rex
R
D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D048271:Chitosan / Q000737:chemistry*; D006868:Hydrolysis; D012995:Solubility; D013025:Glycine max / Q000201:enzymology; D014867:Water / Q000737:chemistry
D014867:Water; D048271:Chitosan; D002688:Chitinases