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Recent advances in β-galactosidase and fructosyltransferase immobilization technology
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Orientador(es)
Resumo(s)
The 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.
Descrição
Palavras-chave
b-galactosidase Immobilization methods Fructosyltransferase Supports . Faculdade de Ciências Exatas e da Engenharia Centro de Química da Madeira
Contexto Educativo
Citação
Filipe Pires, Paula Cristina Castilho & Andrea Gomez-Zavaglia (2021) Recent advances in β galactosidase and fructosyltransferase immobilization technology, Critical Reviews in Food Science and Nutrition, 61:16, 2659-2690, DOI: 10.1080/10408398.2020.1783639
Editora
Taylor and Francis Group