α-L-Fucosidase from bovine kidney

ammonium sulfate suspension, ≥2.0 units/mg protein (biuret)

α-L-Fucoside fucohydrolase
Enzyme Commission number:
MDL number:

Quality Level


ammonium sulfate suspension

specific activity

≥2.0 units/mg protein (biuret)

mol wt

210-220 kDa (Subunits: 55-60 kDa)

foreign activity

α-mannosidase and β-galactosidase ≤0.1%
β-N-acetylglucosaminidase ≤0.2%

shipped in

wet ice

storage temp.


Related Categories

General description

α-L-fucosidases is a liposomal enzyme, which belongs to glycosyl hydrolases family.


α-L-fucosidase from bovine kidney has been used:
  • to study their ability to alter primary cell transduction
  • to examine the role of fucose residues of cell surface glycans in adhesion
  • to investigate its role during fertilization

Biochem/physiol Actions

α-L-fucosidases degrades fucose-containing fucoglycoconjugates and breaks fucosidic bonds in oligosaccharides and glycoconjugates. It acts as a tumor marker for hepatic and colorectal cancer. α-L-fucosidase exhibits transglycosylation property.

Unit Definition

One unit will hydrolyze 1.0 μmole of p-nitrophenyl α-L-fucoside to p-nitrophenol and L-fucose per min at pH 5.5 at 25°C.

Physical form

Suspension in 3.2 M (NH4)2SO4, 10 mM NaH2PO4 10 mM citrate, pH 6.0


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Directed evolution of the alpha-L-fucosidase from Thermotoga maritima into an alpha-L-transfucosidase
Osanjo G, et al.
Biochemistry, 46(4), 1022-1033 (2007)
Human alpha-L-fucosidase-1 attenuates the invasive properties of thyroid cancer
Vecchio G, et al.
Testing, 8(16), 27075-27075 (2017)
Novel alpha-l-fucosidases from a soil metagenome for production of fucosylated human milk oligosaccharides
Lezyk M, et al.
PLoS ONE, 11(1), e0147438-e0147438 (2016)
Markus Günl et al.
The Plant cell, 23(11), 4025-4040 (2011-11-15)
An Arabidopsis thaliana mutant with an altered structure of its hemicellulose xyloglucan (XyG; axy-8) identified by a forward genetic screen facilitating oligosaccharide mass profiling was characterized. axy8 exhibits increased XyG fucosylation and the occurrence of XyG fragments not present in...
Alexis Kotland et al.
The Journal of organic chemistry, 76(10), 4094-4098 (2011-04-19)
The total synthesis of enantiopure 4-epi-(+)-codonopsinine was achieved in 10 steps starting from D-ribose as a chiral building block. The key step involved a highly stereoselective nucleophilic addition of a Grignard reagent to a protected ribosylamine. Synthesis of the N-desmethyl...
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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