Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed Reactor
Flow processes and enzyme immobilization have gained much attention over the past few years in the field of biocatalytic process design. Downstream processes and enzyme stability can be immensely simplified and improved. In this work, we report the utilization of polymer network-entrapped enzymes an...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2019-10-01
|
| Series: | Bioengineering |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2306-5354/6/4/99 |
| _version_ | 1797722095993487360 |
|---|---|
| author | Niklas Adebar Harald Gröger |
| author_facet | Niklas Adebar Harald Gröger |
| author_sort | Niklas Adebar |
| collection | DOAJ |
| description | Flow processes and enzyme immobilization have gained much attention over the past few years in the field of biocatalytic process design. Downstream processes and enzyme stability can be immensely simplified and improved. In this work, we report the utilization of polymer network-entrapped enzymes and their applicability in flow processes. We focused on the superabsorber-based immobilization of an alcohol dehydrogenase (ADH) from <i>Lactobacillus brevis</i> and its application for a reduction of acetophenone. The applicability of this immobilization technique for a biotransformation running in a packed bed reactor was then demonstrated. Towards this end, the immobilized system was intensively studied, first in a batch mode, leading to >90% conversion within 24 h under optimized conditions. A subsequent transfer of this method into a flow process was conducted, resulting in very high initial conversions of up to 67% in such a continuously running process. |
| first_indexed | 2024-03-12T09:42:37Z |
| format | Article |
| id | doaj.art-e01113dbac9549e6af918abc4ff566b0 |
| institution | Directory Open Access Journal |
| issn | 2306-5354 |
| language | English |
| last_indexed | 2024-03-12T09:42:37Z |
| publishDate | 2019-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Bioengineering |
| spelling | doaj.art-e01113dbac9549e6af918abc4ff566b02023-09-02T13:08:59ZengMDPI AGBioengineering2306-53542019-10-01649910.3390/bioengineering6040099bioengineering6040099Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed ReactorNiklas Adebar0Harald Gröger1Chair of Industrial Organic Chemistry and Biotechnology, Faculty of Chemistry, Bielefeld University, Universitätsstr. 25, 33615 Bielefeld, GermanyChair of Industrial Organic Chemistry and Biotechnology, Faculty of Chemistry, Bielefeld University, Universitätsstr. 25, 33615 Bielefeld, GermanyFlow processes and enzyme immobilization have gained much attention over the past few years in the field of biocatalytic process design. Downstream processes and enzyme stability can be immensely simplified and improved. In this work, we report the utilization of polymer network-entrapped enzymes and their applicability in flow processes. We focused on the superabsorber-based immobilization of an alcohol dehydrogenase (ADH) from <i>Lactobacillus brevis</i> and its application for a reduction of acetophenone. The applicability of this immobilization technique for a biotransformation running in a packed bed reactor was then demonstrated. Towards this end, the immobilized system was intensively studied, first in a batch mode, leading to >90% conversion within 24 h under optimized conditions. A subsequent transfer of this method into a flow process was conducted, resulting in very high initial conversions of up to 67% in such a continuously running process.https://www.mdpi.com/2306-5354/6/4/99alcohol dehydrogenaseenzyme immobilizationflow chemistryprocess design |
| spellingShingle | Niklas Adebar Harald Gröger Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed Reactor Bioengineering alcohol dehydrogenase enzyme immobilization flow chemistry process design |
| title | Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed Reactor |
| title_full | Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed Reactor |
| title_fullStr | Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed Reactor |
| title_full_unstemmed | Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed Reactor |
| title_short | Flow Process for Ketone Reduction Using a Superabsorber-Immobilized Alcohol Dehydrogenase from <i>Lactobacillus brevis</i> in a Packed-Bed Reactor |
| title_sort | flow process for ketone reduction using a superabsorber immobilized alcohol dehydrogenase from i lactobacillus brevis i in a packed bed reactor |
| topic | alcohol dehydrogenase enzyme immobilization flow chemistry process design |
| url | https://www.mdpi.com/2306-5354/6/4/99 |
| work_keys_str_mv | AT niklasadebar flowprocessforketonereductionusingasuperabsorberimmobilizedalcoholdehydrogenasefromilactobacillusbrevisiinapackedbedreactor AT haraldgroger flowprocessforketonereductionusingasuperabsorberimmobilizedalcoholdehydrogenasefromilactobacillusbrevisiinapackedbedreactor |