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Part of the book series: Advances in Inclusion Science ((AIS,volume 1))

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Summary

It is known that the methylated analogues of β-cyclodextrin dissolve in cold water 10–20 times better than β-cyclodextrin itself and have good complex-forming property.

It has been investigated how these cyclodextrin derivatives influence the activity of some enzymes.

The results of the experiments with lipase indicate that the rate of glyceride-hydrolysis is higher in the aqueous solution of dimethyl-β-cyclodextrin (10 %) than in the presence of the bile as a natural emulgeator.

The activity of the alkaline phosphatase rises both in the presence of β-cyclodextrin and dimethyl-β-cyclodextrin.

In the case of α-amylase (from Aspergillus oryzae) the in-hibition of the activity by dimethyl-β-cyclodextrin is similar as that of β-cyclodextrin.

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© 1982 Springer Science+Business Media Dordrecht

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Jodál, I. (1982). Enzymatic Investigations with Cyclodextrins. In: Szejtli, J. (eds) Proceedings of the First International Symposium on Cyclodextrins. Advances in Inclusion Science, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-7855-3_17

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  • DOI: https://doi.org/10.1007/978-94-009-7855-3_17

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-009-7857-7

  • Online ISBN: 978-94-009-7855-3

  • eBook Packages: Springer Book Archive

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