EN
Structural and functional catalytic
characteristics of cross-linked enzyme aggregates
(CLEA) are reviewed. Firstly, advantages of enzyme
immobilization and existing types of immobilization
are described. Then, a wide description of the factors
that modify CLEA activity, selectivity and stability is
presented. Nowadays CLEA offers an economic, simple
and easy tool to reuse biocatalysts, improving their
catalytic properties and stability. This immobilization
methodology has been widely and satisfactorily tested
with a great variety of enzymes and has demonstrated
its potential as a future tool to optimize biocatalytic
processes.