Multi-substrate kinetic resolution screening method for lipase biocatalysts

Marton Osze, Diána Weiser, Gábor Hornyánszky, L. Poppe

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Development of efficient screening methods has increasing significance in rapid evaluation of novel biocatalysts. Our study reveals the scopes and limitations of a novel GC-based multi-substrate screening method for initial characterization of the activity and selectivity of lipase biocatalysts. The multi-substrate kinetic resolution of four different racemic alcohols 1-4a by native and immobilized biocatalysts were analyzed by GC using enantiomer selective stationary phase.

Original languageEnglish
Pages (from-to)129-137
Number of pages9
JournalStudia Universitatis Babes-Bolyai Chemia
Issue number2
Publication statusPublished - 2012

Fingerprint

Lipase
Screening
Kinetics
Substrates
Enzymes
Enantiomers
Alcohols

Keywords

  • Biocatalysis
  • Immobilization
  • Lipase
  • Multi-substrate screening

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Multi-substrate kinetic resolution screening method for lipase biocatalysts. / Osze, Marton; Weiser, Diána; Hornyánszky, Gábor; Poppe, L.

In: Studia Universitatis Babes-Bolyai Chemia, No. 2, 2012, p. 129-137.

Research output: Contribution to journalArticle

Osze, Marton ; Weiser, Diána ; Hornyánszky, Gábor ; Poppe, L. / Multi-substrate kinetic resolution screening method for lipase biocatalysts. In: Studia Universitatis Babes-Bolyai Chemia. 2012 ; No. 2. pp. 129-137.
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