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Current Nutrition & Food Science

Editor-in-Chief

ISSN (Print): 1573-4013
ISSN (Online): 2212-3881

Hydrolysis of Galactosylsucrose (lactosucrose) and the Mechanism of Monosaccharide Release by Small Intestinal Enzymes in Human and Rat

Author(s): Sadako Nakamura, Yuko Ide-Zaitsu, Fumio Shimura and Tsuneyuki Oku

Volume 11, Issue 1, 2015

Page: [53 - 59] Pages: 7

DOI: 10.2174/1573401311666150313231231

Price: $65

Abstract

The health benefits of oligosaccharides should be accurately offered to the consumer based on scientific evidence. In particular, the prebiotic effect of nondigestible oligosaccharide is concerned with the digestibility and fermentability in the gastrointestinal tract. Since galactosylsucrose is resistant to the digestion in the gastrointestinal tract, it is widely used as a prebiotic. But, it is still unknown whether it is partially hydrolyzed by small intestinal enzymes. This is the first report that galactosylsucrose is slowly hydrolyzed by human small intestinal enzymes. The present study investigated the hydrolysis of galactosylsucrose using human and rat small intestinal enzymes. Galactosylsucrose was slowly hydrolyzed by small intestinal enzymes from both humans and rats, although the hydrolyzing activity was lower than that for lactose. Galactose, which is bonded via a β-4, 1 linkage to the glucose residue of sucrose, was the first moiety to be released from galactosylsucrose; this increased linearly during the incubation. Glucose and fructose produced from sucrose (which is the hydrolyzed residue of galactosylsucrose) also increased linearly after a delay during the early period of incubation. These results suggest that initially lactase attacks the lactose unit of galactosylsucrose, and sucrase then hydrolyzes the resulting sucrose unit. Thus, hydrolysis of galactosylsucrose starts from the β-4,1-linkage between galactose and glucose at the non-reducing terminal.

Keywords: Galactosylsucrose, hydrolysis, lactosucrose, monosaccharide, human small intestinal enzymes.

Graphical Abstract


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