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Globally, ∼70% of adults are deficient in intestinal lactase, the enzyme required for the digestion of lactose. In these individuals, the consumption of lactose-containing milk and dairy products can lead to the development of various gastrointestinal (GI) symptoms. The primary solution to lactose intolerance is withdrawing lactose from the diet either by eliminating dairy products altogether or substituting lactose-free alternatives. However, studies have shown that certain individuals erroneously attribute their GI symptoms to lactose and thus prefer to consume lactose-free products. This has raised the question whether consuming lactose-free products reduces an individual's ability to absorb dietary lactose and if lactose-absorbers should thus avoid these products. This review summarizes the current knowledge regarding the acclimatization of lactose processing in humans. Human studies that have attempted to induce intestinal lactase expression with different lactose feeding protocols have consistently shown lack of enzyme induction. Similarly, withdrawing lactose from the diet does not reduce intestinal lactase expression. Evidence from cross-sectional studies shows that milk or dairy consumption is a poor indicator of lactase status, corroborating the results of intervention studies. However, in lactase-deficient individuals, lactose feeding supports the growth of lactose-digesting bacteria in the colon, which enhances colonic lactose processing and possibly results in the reduction of intolerance symptoms. This process is referred to as colonic adaptation. In conclusion, endogenous lactase expression does not depend on the presence of dietary lactose, but in susceptible individuals, dietary lactose might improve intolerance symptoms via colonic adaptation. For these individuals, lactose withdrawal results in the loss of colonic adaptation, which might lower the threshold for intolerance symptoms if lactose is reintroduced into the diet.
This article was published in the following journal.
Name: The American journal of clinical nutrition
Lactase is an enzyme that hydrolyzes lactose into glucose and galactose in the small intestine, where they are absorbed. Hypolactasia is a common condition, primarily caused by genetic programming, th...
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The multifunctional protein that contains two enzyme domains. The first domain (EC 220.127.116.11) hydrolyzes glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. The second domain (EC 18.104.22.168) hydrolyzes LACTOSE and is found in the intestinal brush border membrane. Loss of activity for this enzyme in humans results in LACTOSE INTOLERANCE.
The condition resulting from the absence or deficiency of LACTASE in the MUCOSA cells of the GASTROINTESTINAL TRACT, and the inability to break down LACTOSE in milk for ABSORPTION. Bacterial fermentation of the unabsorbed lactose leads to symptoms that range from a mild indigestion (DYSPEPSIA) to severe DIARRHEA. Lactose intolerance may be an inborn error or acquired.
An enzyme which catalyzes the hydrolysis of LACTOSE to D-GALACTOSE and D-GLUCOSE. Defects in the enzyme cause LACTOSE INTOLERANCE.
Allergic reaction to milk (usually cow's milk) or milk products. MILK HYPERSENSITIVITY should be differentiated from LACTOSE INTOLERANCE, an intolerance to milk as a result of congenital deficiency of lactase.
The enzyme hydrolyzing glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. It also catalyzes the hydrolysis of phlorizin to phloretin and glucose. It is found in the intestinal brush border membrane often in conjunction with lactase. EC 22.214.171.124.
Enzymes are proteins that catalyze (i.e., increase the rates of) chemical reactions. In enzymatic reactions, the molecules at the beginning of the process, called substrates, are converted into different molecules, called products. Almost all chemical re...