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Lactase (EC 3.2.1.108) is an enzyme produced by many organisms and is essential to the complete digestion of whole milk. It breaks down the sugar lactose into its component parts, galactose and glucose. Lactase is found in the brush border of the small intestine of humans and other mammals.
(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 breaks down lactose specifically.) β-Galactosides include carbohydrates containing galactose where the glycosidic bond lies above the galactose molecule.
The lactose operon (lac operon) is an operon required for the transport and metabolism of lactose in E. coli and many other enteric bacteria.Although glucose is the preferred carbon source for most enteric bacteria, the lac operon allows for the effective digestion of lactose when glucose is not available through the activity of β-galactosidase. [1]
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The lactase enzyme has two active sites which break down lactose. The first is at Glu1273 and the second is at Glu1749, which separately break down lactose into two separate kinds of molecules. [1] At least six mutations (single-nucleotide polymorphisms – SNPs) have been associated with lactase expression. [28]
On the other hand, the enzyme corresponding to beta-galactosides is called beta-galactosidase; it breaks down the disaccharide lactose for instance, into its monosaccharide components, glucose and galactose. [1] Both varieties of galactosidase are categorized under the EC number 3.2.1.
The hydrolysis of lactose to glucose and galactose is catalyzed by the enzymes lactase and β-galactosidase. The latter is produced by the lac operon in Escherichia coli. [13] In nature, lactose is found primarily in milk and milk products. Consequently, various food products made with dairy-derived ingredients can contain lactose. [14]
The amount of insulin released in the blood and sensitivity of the cells to the insulin both determine the amount of glucose that cells break down. [4] Increased levels of glucagon activates the enzymes that catalyze glycogenolysis, and inhibits the enzymes that catalyze glycogenesis. [15]