Abstract
The enzymatic digestibility of parent γ-cyclodextrin by human saliva α-amylase was investigated aiming at the determination of lifespan of intact macro ring. It was found that the ring-opening reaction was the slowest step of the γ-cyclodextrin degradation process. The reaction products were mainly maltose and malto-triose, while no higher malto-oligomers were detected. The enzymatic degradation of γ-cyclodextrin reduces the possibility of influencing bioavailability of nutritional lipophiles or drug actives co-administered with γ-cyclodextrin as an excipient or additive. Though there are numerous papers on the ring opening of cyclodextrins by amylases and the same capability of the human α-amylase is expected now we prove this activity. The hydrolysis reaction was followed by direct measurement of the resulting maltose and malto-triose, for the first time.
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Harangi, J., Béke, G., Harangi, M. et al. The digestable parent cyclodextrin. J Incl Phenom Macrocycl Chem 73, 335–339 (2012). https://doi.org/10.1007/s10847-011-0061-0
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DOI: https://doi.org/10.1007/s10847-011-0061-0