Enabling industrial biocatalytic processes by application of silicone-coated enzyme preparations

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • René Nieguth - , Technical University of Berlin (First author)
  • Marrit Eckstein - (Author)
  • Oliver Thum - (Author)
  • Marion Bettina Ansorge-Schumacher - , Technical University of Berlin (Author)

Abstract

Composite particles of the commercial lipase preparation NZ435 and silicone (silcoat-NZ435) have recently been described as promising biocatalysts for synthetic use. In this study, their actual potential for enhanced performance in industrial applications was evaluated, focusing on scenarios where carrier disintegration and catalyst leaching constitute key limitations. All three investigated model reactions, the syntheses of myristyl myristate, poly(ethylene glycol) 400-coconut fatty acid monoester and ethylene oxide and propylene oxide co-polymer (EO/PO)-oleic acid diester, were considerably improved in terms of the maximal number of reaction cycles performed with the same batch of catalyst, and consequently in terms of the obtainable product amount. The total turnover numbers (TTN) increased by a factor up to 50, making the realization of this type of reactions in an industrial process more feasible. The utility of silcoat-NZ435 for stereoselective transformations was demonstrated with the enantioselective acylation of 1-phenylethanol with vinyl butyrate, in which full retention of the excellent stereoselectivity of native NZ435 was observed. Moreover, it was demonstrated for the first time that
the methodology by which silcoat-catalysts are obtained can be successfully transferred to alternative carriers and enzymes (e.g., protease, esterase and laccase), opening a broad field for the implementation and advancement of biocatalysis in industrial processes.

Details

Original languageEnglish
Pages (from-to)2522-2528
JournalAdvanced synthesis & catalysis
Volume2011
Issue number353
Publication statusPublished - 2011
Peer-reviewedYes
Externally publishedYes

External IDs

Scopus 80052802797
ORCID /0000-0002-2912-546X/work/171551977

Keywords

Keywords

  • Biokatalyse, Emollientester, Lipase, silCoat, Immobilisierung