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  • Title: Analysis of hydrolytic activity of a 65-kDa chitinase from the silkworm, Bombyx mori.
    Author: Abdel-Banat BM, Zhou W, Karasuda S, Koga D.
    Journal: Biosci Biotechnol Biochem; 2002 May; 66(5):1119-22. PubMed ID: 12092826.
    Abstract:
    The hydrolytic reactions of Bombyx mori 65-kDa chitinase with the short substrates, N-acetyl-chitooligosaccharides, were analyzed by HPLC. Analysis of the hydrolyzed products showed that the newly produced oligosaccharides are all beta anomers, suggesting that, similar to other family 18 glycosyl hydrolases, the 65-kDa chitinase acts in the retaining mechanism. Furthermore, the enzyme cleaves the N-acetylchitooligosaccharides mainly at the linkage between the second and the third GlcNAc moieties from the non-reducing end, while the other sites were cleaved in smaller proportions. Moreover, the initial reaction rates of the enzyme with the longer N-acetylchitooligosaccharides were higher than those with shorter ones. These results suggest that the enzyme is an endo-cleaving type and more efficient on the longer substrates.
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