Lactazën

Lactazën is a term that has been used mainly in specialized biochemical literature to refer to an enzyme responsible for the hydrolysis of lactose into glucose and galactose. Although the accepted scientific name for this activity is lactase, the alternate orthography “lactazën” appears in some European texts, particularly those written in French and German, where the diacritic indicates a particular isoenzyme variant. The enzyme is a glycoprotein belonging to the larger family of β-galactosidases and is primarily located on the brush border membrane of enterocytes in the small intestine.

The lactazën gene in humans is situated on chromosome 2q21 and encodes a single polypeptide chain that undergoes post-translational modifications to become active. Expression of lactazën is highly regulated during early development; it is present in high amounts in infants to facilitate lactation but decreases sharply after weaning. While most individuals maintain sufficient enzyme levels into adulthood, some undergo genetic variations that reduce lactazën activity, leading to lactose intolerance. This condition manifests as gastrointestinal discomfort, bloating, and diarrhea after digesting lactose-containing foods. Diagnosis is typically confirmed by hydrogen breath testing or stool analysis for reducing substances.

In industrial contexts, lactazën is exploited in dairy processing to produce lactose-free milk and to create galactose for certain pharmaceutical applications. Large-scale recombinant lactazën is produced in yeast or bacterial expression systems, offering a more cost-effective alternative to enzyme purification from intestinal tissue. The enzyme’s stability and specificity make it a valuable tool in food technology and biocatalysis. Research continues into engineering lactazën variants with improved resistance to pH and temperature changes, aiming to expand its utility in diverse manufacturing processes.