Encapsulation of crosslinked penicillin G acylase aggregates in lentikats: Evaluation of a novel biocatalyst in organic media

LORENA EVELYN WILSON SOTO, Andrés Illanes, Benevides C.C. Pessela, Olga Abian, Roberto Fernández-Lafuente, José M. Guisán

Research output: Contribution to journalArticlepeer-review

116 Scopus citations

Abstract

The encapsulation of crosslinked enzyme aggregates (CLEA) of penicillin G acylase into a very rigid polymeric matrix based on polyvinyl alcohol (LentiKats) has been used successfully to improve the inadequate mechanical properties of CLEA. This encapsulation decreased CLEA activity by only around 40%. As compensation, a significant improvement in the stability of the CLEA in the presence of organic solvents was detected. This could be related to the highly hydrophilic environment inside the LentiKats biocatalysts: Partition experiments showed that the concentration of dioxane inside LentiKats was lower than in the reaction medium. In fact, thermal stability was about the same as in the corresponding CLEA. This permitted great improvement in the reaction rate for thermodynamically controlled synthesis of a model antibiotic (using phenylacetic acid and 7-amino-deacetoxycefalosporanic acid). Even more importantly, yields could be improved by using LentiKats-encapsulated CLEA, very likely by a favorable product/substrate partition. Thus, this very simple technique not only provides an efficient technique for solving the mechanical stability problem associated with CLEA, but also greatly improves the behavior of CLEA in organic media.

Original languageEnglish
Pages (from-to)558-562
Number of pages5
JournalBiotechnology and Bioengineering
Volume86
Issue number5
DOIs
StatePublished - 5 Jun 2004
Externally publishedYes

Keywords

  • Crosslinked enzyme aggregates
  • Entrapment
  • Enzymes in organic solvents
  • Hydrogel
  • Immobilization
  • LentiKats
  • Penicillin acylase
  • Polyvinyl alcohol

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