Β-Galactosidase: Difference between revisions

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{{Short description|Enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides}}
{{Short description|Enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides}}
{{Infobox enzyme
| name = β-Galactosidase
| image = Beta-Galactosidase 1JYN.png
| caption = Structure of β-galactosidase enzyme
| EC_number = 3.2.1.23
| CAS_number = 9031-11-2
| IUBMB_EC_number = 3/2/1/23
| GO_code = 0004565
}}


'''β-Galactosidase''' (β-gal) is an [[enzyme]] that catalyzes the hydrolysis of [[β-galactosides]] into their constituent [[monosaccharides]]. It is an essential enzyme in carbohydrate metabolism and is commonly found in [[bacteria]], [[fungi]], and [[mammals]]. In humans, a deficiency in β-galactosidase activity is associated with certain [[lysosomal storage disorders]].
'''β-Galactosidase''' (β-gal) is an [[enzyme]] that catalyzes the hydrolysis of [[β-galactosides]] into their constituent [[monosaccharides]]. It is an essential enzyme in carbohydrate metabolism and is commonly found in [[bacteria]], [[fungi]], and [[mammals]]. In humans, a deficiency in β-galactosidase activity is associated with certain [[lysosomal storage disorders]].

Latest revision as of 09:17, 14 March 2025

Enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides


β-Galactosidase (β-gal) is an enzyme that catalyzes the hydrolysis of β-galactosides into their constituent monosaccharides. It is an essential enzyme in carbohydrate metabolism and is commonly found in bacteria, fungi, and mammals. In humans, a deficiency in β-galactosidase activity is associated with certain lysosomal storage disorders.

Function[edit]

β-Galactosidase hydrolyzes β-galactosides, breaking the glycosidic bond between a galactose molecule and its linked sugar. This enzyme plays a crucial role in:

Biochemical Properties[edit]

  • Enzyme classification: EC 3.2.1.23
  • Substrates: β-galactosides, including lactose.
  • Products: Monosaccharides such as glucose and galactose.
  • Cofactors: Metal ions like Mg²⁺ may enhance activity.
  • Optimal pH: Varies by species, commonly around pH 6–8.

β-Galactosidase in Bacteria[edit]

In Escherichia coli (E. coli), β-galactosidase is encoded by the lacZ gene, part of the lac operon. This enzyme allows E. coli to metabolize lactose when glucose is unavailable.

The lac operon consists of:

  • lacZ – Encodes β-galactosidase.
  • lacY – Encodes lactose permease, which transports lactose into the cell.
  • lacA – Encodes thiogalactoside transacetylase, with an unclear role in lactose metabolism.

β-Galactosidase in E. coli can be measured using X-gal, which produces a blue color when hydrolyzed, a key feature in blue-white screening used in molecular biology.

β-Galactosidase in Humans[edit]

In humans, β-galactosidase is found in the lysosome and is responsible for breaking down glycosphingolipids. Mutations in the GLB1 gene lead to:

Industrial and Clinical Applications[edit]

β-Galactosidase has various applications in:

  • Dairy industry – Used in lactose-free milk production.
  • Molecular biology – Utilized in blue-white screening for detecting recombinant plasmids.
  • Medical diagnostics – Studied for enzyme replacement therapies in lysosomal storage disorders.

Related Enzymes[edit]

See Also[edit]