Fucosidase Alpha-L-1 plays a crucial role in the degradation of fucose-containing glycoconjugates. It catalyzes the hydrolysis of terminal L-fucose residues linked via alpha-1,2, alpha-1,3, alpha-1,4, or alpha-1,6 linkages . This activity is essential for various biological processes, including cell-cell interaction, signal transduction, and immune response.
The enzyme’s activity is measured by its ability to cleave a fluorogenic substrate, 4-methylumbelliferyl-alpha-L-fucopyranoside. The specific activity of the recombinant enzyme is greater than 550 pmol/min/μg under the described conditions .
Alpha-L-fucosidase has significant clinical implications. It is used as a serum marker for the diagnosis of hepatocellular carcinoma (HCC), a common type of liver cancer . Additionally, deficiencies in this enzyme can lead to a rare lysosomal storage disorder known as fucosidosis, characterized by the accumulation of fucose-containing glycolipids and glycoproteins in various tissues.
The recombinant human plasma alpha-L-fucosidase is produced with an N-terminal 6-His tag, which facilitates its purification. The enzyme is highly pure, with a purity greater than 95% as determined by SDS-PAGE and visualized by Coomassie® Blue staining . It is also important to note that the endotoxin level is kept below 0.10 EU per 1 μg of the protein, ensuring its safety for research and therapeutic applications .