Journal
REACTION CHEMISTRY & ENGINEERING
Volume 6, Issue 12, Pages 2391-2399Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1re00342a
Keywords
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Funding
- National Research Development and Innovation (NRDI) Fund (TKP2020 IES) under Ministry for Innovation and Technology, Hungary
- NRDI Office [PD-131467]
- Collegium Talentum 2020 Programme of Hungary
- project: Entrepreneurship for innovation through doctoral and postdoctoral research - European Social Fund, through the Operation Program for Human Capital 2014-2020 [POCU/380/6/13/123886]
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An efficient nanobioconjugate of lipase B was prepared and tested for the enzymatic kinetic resolution of racemic secondary 1-arylethan-1-ols. Various process parameters were investigated to determine the conditions for highest productivity, enabling hundred gram scale resolution with minimal biocatalyst usage. The long-term activity and selectivity of the biocatalyst were preserved throughout the study.
An efficient nanobioconjugate of lipase B from Candida antarctica was prepared by covalent binding onto carboxy-functionalized single-walled carbon nanotubes and tested in batch and flow modes for the enzymatic kinetic resolution of several racemic secondary 1-arylethan-1-ols. The influence of various process parameters such as temperature, flow rate and substrate concentration upon the biocatalyst efficiency and selectivity in the kinetic resolution of rac-1-phenylethan-1-ol was investigated and the conditions for the highest productivity were determined. The long-term activity and selectivity of the biocatalyst were preserved, enabling hundred gram scale resolution of rac-1-phenylethan-1-ol with only similar to 70 mg of biocatalyst.
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