Surface Immobilization and Shielding of a Transaminase Enzyme for the Stereoselective Synthesis of Pharmaceutically Relevant Building Blocks
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Authors
Author (Corporation)
Publication date
05/2018
Typ of student thesis
Course of study
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Type
01A - Journal article
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Parent work
Chimia
Special issue
DOI of the original publication
Link
Series
Series number
Volume
72
Issue / Number
5
Pages / Duration
345-346
Patent number
Publisher / Publishing institution
Schweizerische Chemische Gesellschaft
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Abstract
Transaminases are enzymes capable of stereoselective reductive amination; they are of great interest in the production of chiral building blocks. However, the use of this class of enzymes in industrial processes is often hindered by their limited stability under operational conditions. Herein, we demonstrate that a transaminase enzyme from Aspergillus terreus can be immobilized at the surface of silica nanoparticles and protected in an organosilica shell of controlled thickness. The so-protected enzyme displays a high biocatalytic activity, and additionally provides the possibility to be retained in a reactor system for continuous operation and to be recycled.
Keywords
Chiral building blocks, Transaminases
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ISBN
ISSN
2673-2424
0009-4293
0009-4293
Language
English
Created during FHNW affiliation
Yes
Strategic action fields FHNW
Publication status
Published
Review
Peer review of the complete publication
Open access category
License
Citation
Alami, A. T., Richina, F., Hernandez, M., Dudal, Y., & Shahgaldian, P. (2018). Surface Immobilization and Shielding of a Transaminase Enzyme for the Stereoselective Synthesis of Pharmaceutically Relevant Building Blocks. Chimia, 72(5), 345–346. https://doi.org/10.2533/chimia.2017.345