Cross-linked enzyme aggregates (CLEA) in enzyme improvement – a review

  • Velasco-Lozano S
  • López-Gallego F
  • Mateos-Díaz J
  • et al.
N/ACitations
Citations of this article
223Readers
Mendeley users who have this article in their library.

Abstract

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.

Cite

CITATION STYLE

APA

Velasco-Lozano, S., López-Gallego, F., Mateos-Díaz, J. C., & Favela-Torres, E. (2016). Cross-linked enzyme aggregates (CLEA) in enzyme improvement – a review. Biocatalysis, 1(1). https://doi.org/10.1515/boca-2015-0012

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free