Everything about Lactase totally explained
Lactase (LCT), a member 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.
Industrial use
Lactase produced commercially can be extracted both from
yeasts such as
Kluyveromyces fragilis and
Kluyveromyces lactis and from
fungi, such as
Aspergillus niger and
Aspergillus oryzae. Its primary commercial use is to break down lactose in milk to make it suitable for people with
lactose intolerance. Lactase is also used in the manufacture of
ice cream. Because glucose and galactose are sweeter than lactose, lactase produces a more pleasant taste. Lactose also crystallises at the low temperatures of ice cream; however, its constituent products stay liquid and contribute to a smoother texture. Lactase is used in the conversion of
whey into syrup.
Lactase is also used to screen for blue white colonies into the MCS of various plasmid vectors in
Escherichia coli or other bacteria.
Further Information
Get more info on 'Lactase'.
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