TY - JOUR
T1 - Hydroxynitrile lyases covalently immobilized in continuous flow microreactors
AU - Van Der Helm, Michelle P.
AU - Bracco, Paula
AU - Busch, Hanna
AU - Szymańska, Katarzyna
AU - Jarzȩbski, Andrzej B.
AU - Hanefeld, Ulf
PY - 2019
Y1 - 2019
N2 -
Enzymes are supreme catalysts when it comes to high enantiopurities and their immobilization will pave the way for continuous operation. In this context, we show the covalent immobilization of hydroxynitrile lyases HbHNL (from Hevea brasiliensis) and MeHNL (from Manihot esculenta) in a siliceous monolithic microreactor for continuous operation. A thorough characterization of the immobilized HNLs on mesoporous silicates indicated the conditions essential for a successful immobilization. Their application in a continuous flow system enabled a remarkably fast (3.2 min) production of chiral cyanohydrins with high conversion (97%) and high ee (98%) using minimal enzyme loading (STY = 71 g L
-1
h
-1
mg
protein
-1
). MeHNL showed increased operational stability, possibly due to a structural difference. The continuous flow microreactor outperformed batch systems, demonstrating the advantage of the mesoporous/macroporous environment for the expression of enzyme activity and the favorable characteristics of the microreactor. Overall, the system shows great potential for future industrial application of biocatalytic asymmetric syntheses.
AB -
Enzymes are supreme catalysts when it comes to high enantiopurities and their immobilization will pave the way for continuous operation. In this context, we show the covalent immobilization of hydroxynitrile lyases HbHNL (from Hevea brasiliensis) and MeHNL (from Manihot esculenta) in a siliceous monolithic microreactor for continuous operation. A thorough characterization of the immobilized HNLs on mesoporous silicates indicated the conditions essential for a successful immobilization. Their application in a continuous flow system enabled a remarkably fast (3.2 min) production of chiral cyanohydrins with high conversion (97%) and high ee (98%) using minimal enzyme loading (STY = 71 g L
-1
h
-1
mg
protein
-1
). MeHNL showed increased operational stability, possibly due to a structural difference. The continuous flow microreactor outperformed batch systems, demonstrating the advantage of the mesoporous/macroporous environment for the expression of enzyme activity and the favorable characteristics of the microreactor. Overall, the system shows great potential for future industrial application of biocatalytic asymmetric syntheses.
UR - http://www.scopus.com/inward/record.url?scp=85062521947&partnerID=8YFLogxK
U2 - 10.1039/c8cy02192a
DO - 10.1039/c8cy02192a
M3 - Article
AN - SCOPUS:85062521947
SN - 2044-4753
VL - 9
SP - 1189
EP - 1200
JO - Catalysis Science and Technology
JF - Catalysis Science and Technology
IS - 5
ER -