The digestable parent cyclodextrin

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.