Lactase

Lactase is an enzyme produced by many organisms. It is located in the brush border of the small intestine of humans and other mammals. Lactase is essential to the complete digestion of whole milk; it breaks down lactose, a sugar which gives milk its sweetness. Lacking lactase, a person consuming dairy products may experience the symptoms of lactose intolerance. Lactase can be purchased as a food supplement, and is added to milk to produce 'lactose-free' milk products. Lactase is an enzyme produced by many organisms. It is located in the brush border of the small intestine of humans and other mammals. Lactase is essential to the complete digestion of whole milk; it breaks down lactose, a sugar which gives milk its sweetness. Lacking lactase, a person consuming dairy products may experience the symptoms of lactose intolerance. Lactase can be purchased as a food supplement, and is added to milk to produce 'lactose-free' milk products. Lactase (also known as lactase-phlorizin hydrolase, or LPH), 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. Lactase is present predominantly along the brush border membrane of the differentiated enterocytes lining the villi of the small intestine. In humans, lactase is encoded by the LCT gene. Lactase is an enzyme that some people are unable to produce in their small intestine. Without it they can't break down the natural lactose in milk, leaving them with diarrhea, gas and bloating when drinking regular milk. Technology to produce lactose-free milk, ice cream and yogurt was developed by the USDA Agricultural Research Service in 1985. This technology is used to add lactase to milk, thereby hydrolyzing the lactose naturally found in milk, leaving it slightly sweet but digestible by everyone. Without lactase, lactose intolerant people pass the lactose undigested to the colon where bacteria break it down, creating carbon dioxide and that leads to bloating and flatulence. Lactase supplements are sometimes used to treat lactose intolerance. Lactase produced commercially can be extracted both from yeasts such as Kluyveromyces fragilis and Kluyveromyces lactis and from molds, such as Aspergillus niger and Aspergillus oryzae. Its primary commercial use, in supplements such as Lacteeze and Lactaid, is to break down lactose in milk to make it suitable for people with lactose intolerance, However, the U.S. Food and Drug Administration has not formally evaluated the effectiveness of these products. Lactase is also used to screen for blue white colonies in the multiple cloning sites of various plasmid vectors in Escherichia coli or other bacteria. The optimum temperature for human lactase is about 37 °C for its activity and the optimum pH is 6. In metabolism, the β-glycosidic bond in D-lactose is hydrolyzed to form D-galactose and D-glucose, which can be absorbed through the intestinal walls and into the bloodstream. The overall reaction that lactase catalyzes is C12H22O11 + H2O → C6H12O6 + C6H12O6 + heat. The catalytic mechanism of D-lactose hydrolysis retains the substrate anomeric configuration in the products. While the details of the mechanism are uncertain, the stereochemical retention is achieved through a double displacement reaction. Studies of E. coli lactase have proposed that hydrolysis is initiated when a glutamate nucleophile on the enzyme attacks from the axial side of the galactosyl carbon in the β-glycosidic bond. The removal of the D-glucose leaving group may be facilitated by Mg-dependent acid catalysis. The enzyme is liberated from the α-galactosyl moiety upon equatorial nucleophilic attack by water, which produces D-galactose.