Lactase in the context of Β-Galactosidase

Milk is a white liquid food produced by the mammary glands of lactating mammals. It is the primary source of nutrition for young mammals (including breastfed human infants) before they are able to digest solid food. Milk contains many nutrients, including calcium and protein, as well as lactose and saturated fat; the enzyme lactase is needed to break down lactose. Immune factors and immune-modulating components in milk contribute to milk immunity. The first milk, which is called colostrum, contains antibodies and immune-modulating components that strengthen the immune system against many diseases.

As an agricultural product, milk is collected from farm animals, mostly cattle, on a dairy. It is used by humans as a drink and as the base ingredient for dairy products. The US CDC recommends that children over the age of 12 months (the minimum age to stop giving breast milk or formula) should have two servings of milk products a day, and more than six billion people worldwide consume milk and milk products. The ability for adult humans to digest milk relies on lactase persistence, so lactose intolerant individuals have trouble digesting lactose.

Lactose intolerance is caused by a lessened ability or a complete inability to digest lactose, a sugar found in dairy products. Humans vary in the amount of lactose they can tolerate before symptoms develop. Symptoms may include abdominal pain, bloating, diarrhea, flatulence, and nausea. These symptoms typically start thirty minutes to two hours after eating or drinking something containing lactose, with the severity typically depending on the amount consumed. Lactose intolerance does not cause damage to the gastrointestinal tract.

Lactose intolerance is due to the lack of the enzyme lactase in the small intestines to break lactose down into glucose and galactose. There are four types: primary, secondary, developmental, and congenital. Primary lactose intolerance occurs as the amount of lactase declines as people grow up. Secondary lactose intolerance is due to injury to the small intestine. Such injury could be the result of infection, celiac disease, inflammatory bowel disease, or other diseases. Developmental lactose intolerance may occur in premature babies and usually improves over a short period of time. Congenital lactose intolerance is an extremely rare genetic disorder in which little or no lactase is made from birth. The reduction of lactase production starts typically in late childhood or early adulthood, but prevalence increases with age.

Lactase persistence or lactose tolerance is the continued activity of the lactase enzyme in adulthood, allowing the digestion of lactose in milk. In most mammals, the activity of the enzyme is dramatically reduced after weaning. In some human populations though, lactase persistence has recently evolved as an adaptation to the consumption of nonhuman milk and dairy products beyond infancy. Lactase persistence is very high among northern Europeans. Worldwide, most people are lactase non-persistent, and are affected by varying degrees of lactose intolerance as adults. However, lactase persistence and lactose intolerance can overlap.

β-Galactosidase (EC 3.2.1.23, beta-gal or β-gal; systematic name β-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyzes hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides. (This enzyme digests many β-Galactosides, not just lactose. It is sometimes loosely referred to as lactase but that name is generally reserved for mammalian digestive enzymes that break down lactose specifically.)

β-Galactosides include carbohydrates containing galactose where the glycosidic bond lies above the galactose molecule. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins.