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Updated: Oct 30, 2025

Tracing Gene Expression Through Detection of β-galactosidase Activity in Whole Mouse Embryos
Published on: June 26, 2018
Challenges and perspectives of the β-galactosidase enzyme
B I S Damin1, F C Kovalski2, J Fischer3
1Faculty of Agronomy and Veterinary Medicine (FAMV), Postgraduate Program in Food Science and Technology (PPGCTA), University of Passo Fundo (UPF), Passo Fundo, RS, Brazil.
Abstract:
The enzyme β-galactosidase has great potential for application in the food and pharmaceutical industries due to its ability to perform the hydrolysis of lactose, a disaccharide present in milk and in dairy by-products. It can be used in free form, in batch processes, or in immobilized form, which allows continuous operation and provides greater enzymatic stability. The choice of method and support for enzyme immobilization is essential, as the performance of the biocatalyst is strongly influenced by the properties of the material used and by the interaction mechanisms between support and enzyme. Therefore, this review showed the main enzyme immobilization techniques, and the most used supports for the constitution of biocatalysts. Also, materials with the potential for immobilization of β-galactosidases and the importance of their biotechnological application are presented. KEY POINTS: • The main methods of immobilization are physical adsorption, covalent bonding, and crosslinking. • The structural conditions of the supports are determining factors in the performance of the biocatalysts. • Enzymatic hydrolysis plays an important role in the biotechnology industry.
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