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|Stability:||> 10 years under recommended storage conditions|
|Main Chain Glycosidic Linkage:||β-1,4|
|Substrate For (Enzyme):||endo-Chitinase|
High purity Chitin (shrimp shells) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
This substrate is recommended for the assay of endo-chitinase using reducing sugar methods.
Equivalent to Sigma product Chitin from shrimp (#C9752).
Looking for other products? See our polysaccharides product list.
Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity.
Kimura, M., Watanabe, T., Sekine, K., Ishizuka, H., Ikejiri, A., Sakaguchi, M., Kamaya, M., Yamanaka, D., Matoska, V., Bauer, P. O. & Oyama, F. (2020). International Journal of Biological Macromolecules, 164, 2895-2902.
Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due to their involvement in various pathological conditions such as Gaucher's disease and asthma, respectively. Both enzymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, the chitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counterpart. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 against artificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leucine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, the L218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 may compensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplements low Chit1 activity.Hide Abstract
Hoßbach, J., Bußwinkel, F., Kranz, A., Wattjes, J., Cord-Landwehr, S. & Moerschbacher, B. M. (2017). Carbohydrate Polymers, 183, 1-10.
Chitosan is a structurally diverse biopolymer that is commercially derived from chitin by chemical processing, but chitin deacetylases (CDAs) potentially offer a sustainable and more controllable approach allowing the production of chitosans with tailored structures and biological activities. We investigated the CDA from Podospora anserina (PaCDA) which is closely related to Colletotrichum lindemuthianum CDA in the catalytic domain, but unique in having two chitin-binding domains. We produced recombinant PaCDA in Hansenula polymorpha for biochemical characterization and found that the catalytic domain of PaCDA is also functionally similar to C. lindemuthianum CDA, though differing in detail. When studying the enzyme’s mode of action on chitin oligomers by quantitative mass-spectrometric sequencing, we found almost all possible sequences up to full deacetylation but with a clear preference for specific products. Deletion muteins lacking one or both CBDs confirmed their proposed function in supporting the enzymatic conversion of the insoluble substrate colloidal chitin.Hide Abstract