Home > A. Molecular pathology > lactase
lactase
Wednesday 27 May 2009
Lactase (LCT), a part of the β-galactosidase family of enzymes, is a glycoside hydrolase involved in the hydrolysis of the disaccharide lactose into constituent galactose and glucose monomers.
In humans, lactase is present predominantly along the brush border membrane of the differentiated enterocytes lining the villi of the small intestine.
Lactase is essential for digestive hydrolysis of lactose in milk. Deficiency of the enzyme causes lactose intolerance.
The optimum temperature for lactase is about 48 °C (118.4 °F) for its activity and has an optimum pH of 6.5.
The normal mammalian condition is for the young of a species to experience reduced lactase production at the end of the weaning period (a species-specific length of time). In non dairy consuming societies, lactase production usually drops about 90% during the first four years of life, although the exact drop over time varies widely.
However, certain human populations have a mutation on chromosome 2 which eliminates the shutdown in lactase production, making it possible for members of these populations to continue consumption of fresh milk and other dairy products throughout their lives without difficulty. This appears to be an evolutionarily recent adaptation to dairy consumption, and has occurred independently in both northern Europe and east Africa in populations with a historically pastoral lifestyle.
Lactase persistence, allowing lactose digestion to continue into adulthood, is a dominant allele, making lactose intolerance a recessive genetic trait.
Some cultures, such as that of Japan, where dairy consumption has been on the increase, demonstrate a lower prevalence of lactose intolerance in spite of a genetic predisposition.
Pathological lactose intolerance can be caused by Coeliac disease, which damages the villi in the small intestine that produce lactase. This lactose intolerance is temporary. Lactose intolerance associated with coeliac disease ceases after the patient has been on a gluten-free diet long enough for the villi to recover.
Certain people who report problems with consuming lactose are not actually lactose intolerant.
In a study of 323 Sicilian adults, Carroccio et al. (1998) found only 4% were both lactose intolerant and lactose maldigesters, while 32.2% were lactose maldigesters but did not test as lactose intolerant. However, Burgio et al. (1984) found that 72% of 100 Sicilians were lactose intolerant in their study and 106 of 208 northern Italians (i.e., 51%) were lactose intolerant.
Pathology
lactose intolerance