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- Recent advances in β-galactosidase and fructosyltransferase immobilization technologyPublication . Ureta, Maria Micaela; Martins, Gonçalo Nuno; Figueira, Onofre; Pires, Pedro Filipe; Castilho, Paula Cristina; Gomez-Zavaglia, AndreaThe highly demanding conditions of industrial processes may lower the stability and affect the activity of enzymes used as biocatalysts. Enzyme immobilization emerged as an approach to pro mote stabilization and easy removal of enzymes for their reusability. The aim of this review is to go through the principal immobilization strategies addressed to achieve optimal industrial proc esses with special care on those reported for two types of enzymes: b-galactosidases and fructo syltransferases. The main methods used to immobilize these two enzymes are adsorption, entrapment, covalent coupling and cross-linking or aggregation (no support is used), all of them having pros and cons. Regarding the support, it should be cost-effective, assure the reusability and an easy recovery of the enzyme, increasing its stability and durability. The discussion provided showed that the type of enzyme, its origin, its purity, together with the type of immobilization method and the support will affect the performance during the enzymatic synthesis. Enzymes’ immobilization involves interdisciplinary knowledge including enzymology, nanotechnology, molecular dynamics, cellular physiology and process design. The increasing availability of facilities has opened a variety of possibilities to define strategies to optimize the activity and re-usability of b-galactosidases and fructosyltransferases, but there is still great place for innovative developments.