The History of Maltose‐active Disaccharidases

Abstract

The history of maltose-active disaccharidases is closely related to the history of the sugar and starch industry. It began in the 19th century, when a shortage of cane sugar occurred in continental Europe, because Napoleon Bonaparte decreed that no goods could be imported from England to the countries he occupied. Other sugar sources had to be found, and it led to the identification of sugar beets as alternative source of sugar by Marggraf in 1774, to the detection of starch hydrolysis by diluted sulfuric acid by Kirchhoff in 1812, and to the starch digestion enzyme, α-amylase, by Payen in 1833. In the 20th century, Borkström's group in Sweden investigated the absorption of nutrients in human adults by transintubation techniques and found that the luminal concentration of invertase was small compared to that of α-amylase. They speculated that the major locus of this enzyme activity must be in the intestinal cells. Borkström's coworker, Dahlqvist, investigated the maltose-active enzymes in pig intestine, and a second group around Semenza studied the maltase-active enzymes in rabbit intestine. After the first descriptions of congenital sucrase-isomaltase deficiency in 1960 and 1961, the research on disaccharidases increased. Dahlqvist published the first quantitative method to measure these enzymes. Consecutive research led to the discovery of 4 maltases, which were later identified as 2 complex enzymes: the sucrase-isomaltase complex and the maltase-glucoamylase complex. The homology of the 2 enzyme complexes was later determined when the cDNA sequences of the 2 complexes in human intestine were identified.

Review: Nutritional regulation of intestinal starch and protein assimilation in ruminants

“…These four activities are better described as α-glucosidases because they digest multiple linear starch oligosaccharides to glucose, not just maltose. An excellent chronology of the study of intestinal disaccharidases is available (Lentze, 2018).…”

Complementary Starch Feeding of the Young Child

“…Amylase-deficient digestion of starch to absorbable glucose is driven by the mucosal maltases present from birth. The maltase measured in clinical small intestine biopsies is comprised of four activities expressed from two genes; sucraseisomaltase and maltase-glucoamylase (1,2). Glucoamylase produces glucose at a high rate.…”

Characterization and Analysis of Food-Sourced Carbohydrates

“…The nonreducing sugar sucrose, which is composed of glucose and fructose, is the most common sugar present in the human diet, and is responsible for up to 14% of the total energy intake [6]. The disaccharide maltose is formed from two units of glucose and is linked via a ⍺ (1!4) glycosidic bond which can be broken down by the enzyme maltase to release the glucose units [7]. The reducing sugar lactose, which is present in milk and milk products serves as an energy source for infants and can be hydrolyzed by the enzyme β-galactosidase (also known as lactase) into its monosaccharide components, galactose and glucose.…”