Lipase immobilization via cross-linked enzyme aggregates: Problems and prospects - A review

Int J Biol Macromol. 2022 Aug 31:215:434-449. doi: 10.1016/j.ijbiomac.2022.06.139. Epub 2022 Jun 22.

Abstract

In this review we have focused on the preparation of cross-linked enzyme aggregates (CLEAs) from lipases, as these are among the most used enzyme in bioprocesses. This immobilization method is considered very attractive due to preparation simplicity, non-use of supports and the possibility of using crude enzyme extracts. CLEAs provide lipase stabilization under extreme temperature or pH conditions or in the presence of organic solvents, in addition to preventing enzyme leaching in aqueous medium. However, it presents some problems in the preparation and limitations in their use. The problems in preparation refer mainly to the crosslinking step, and may be solved using an aminated feeder. The problems in handling have been tackled designing magnetic-CLEAs or trapping the CLEAs in particles with better mechanical properties, the substrate diffusion problems has been reduced by producing more porous-CLEAs, etc. The enzyme co-immobilization using combi-CLEAs is also a new tendency. Therefore, this review explores the CLEAs methodology aimed at lipase immobilization and its applications.

Keywords: CLEAs application; Crosslinking failure; Mechanical fragility.

Publication types

  • Review

MeSH terms

  • Cross-Linking Reagents / chemistry
  • Enzyme Stability
  • Enzymes, Immobilized* / chemistry
  • Lipase* / chemistry
  • Temperature

Substances

  • Cross-Linking Reagents
  • Enzymes, Immobilized
  • Lipase