Open AccessSurface Immobilization and Shielding of a Transaminase Enzyme for the Stereoselective Synthesis of Pharmaceutically Relevant Building Blocks
Author(s) -
Ayoub Talbi Alami,
Frederica Richina,
M. Rita Correro,
Yves Dudal,
Patrick Shahgaldian
Publication year - 2018
Publication title -
chimia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.387
H-Index - 55
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.2017.345
Subject(s) - aspergillus terreus , stereoselectivity , amination , enzyme , reductive amination , immobilized enzyme , transaminase , chemistry , combinatorial chemistry , materials science , catalysis , chemical engineering , organic chemistry , biochemistry , engineering
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.