SUMMARY: Covalent linkages between chitin and β-glucan in the wall of were indicated by the markedly changed solubility characteristics of the glucan when chitin was specifically removed either (i) by enzymic digestion with purified chitinase or (ii) by first deacetylating the chitin with alkali followed by depolymerization of the deacetylated chitin with nitrous acid. After depolymerization of the chitin, two types of β-glucans could be isolated: one was water-soluble and highly branched, the other was alkali-soluble with branches only one glucose unit long. Lysine (50%) and citrulline (20%) were the major amino acids in the R-glucan/chitin complex. By digesting 90% of the β-glucan in the R-glucan/chitin complex with (1→3)-β-glucanase, a residue was obtained which, on hydrolysis with chitinase, yielded -acetylglucosamine and a compound containing (-acetyl)-glucosamine, lysine and/or citrulline. A model is proposed for the R-glucan/chitin complex in which amino acids, especially lysine and citrulline, are involved in the linkages between glucan and chitin.


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