Biofunctionalized “Kiwifruit‐Assembly” of Oxidoreductases in Mesoporous ZnO/Carbon Nanoparticles for Efficient Asymmetric Catalysis

Biofunctionalized “Kiwifruit‐Assembly” of Oxidoreductases in Mesoporous ZnO/Carbon... A mesoporous ZnO/carbon composite is designed for coimmobilization of two oxidoreductases involving a novel “kiwifruit‐assembly” pattern. The coimmobilization of (S)‐carbonyl reductase II‐glucose dehydrogenase on nanoparticles (SCRII–GDHnano) exhibits 40–50% higher specific activity than the free enzyme and significantly improves stabilities of enzymes to heat, pH and solvents. It performs asymmetric catalysis of 75 × 10−3m substrate with a perfect yield of 100% and an excellent enantioselectivity of 99.9% within 1 h. SCRII–GDHnano gives an over 72% yield and 99.9% enantioselectivity after it is reused for ten times. Even with a highly concentrated (400 × 10−3m) substrate, it shows about 60% yield and 99.9% enantioselectivity within 4 h. SCRII–GDHnano presents 4.5–8.0‐fold higher productivity in 2.0–8.0‐fold shorter reaction time than the free enzyme. This work provides a general, facile, and unique approach for the immobilization of two oxidoreductases and gives high catalytic efficiency, long‐term and good recycling stabilities by triggering radical proton‐coupled electron transfer. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Advanced Materials Wiley

Biofunctionalized “Kiwifruit‐Assembly” of Oxidoreductases in Mesoporous ZnO/Carbon Nanoparticles for Efficient Asymmetric Catalysis

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
© 2018 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim
ISSN
0935-9648
eISSN
1521-4095
D.O.I.
10.1002/adma.201705443
Publisher site
See Article on Publisher Site

Abstract

A mesoporous ZnO/carbon composite is designed for coimmobilization of two oxidoreductases involving a novel “kiwifruit‐assembly” pattern. The coimmobilization of (S)‐carbonyl reductase II‐glucose dehydrogenase on nanoparticles (SCRII–GDHnano) exhibits 40–50% higher specific activity than the free enzyme and significantly improves stabilities of enzymes to heat, pH and solvents. It performs asymmetric catalysis of 75 × 10−3m substrate with a perfect yield of 100% and an excellent enantioselectivity of 99.9% within 1 h. SCRII–GDHnano gives an over 72% yield and 99.9% enantioselectivity after it is reused for ten times. Even with a highly concentrated (400 × 10−3m) substrate, it shows about 60% yield and 99.9% enantioselectivity within 4 h. SCRII–GDHnano presents 4.5–8.0‐fold higher productivity in 2.0–8.0‐fold shorter reaction time than the free enzyme. This work provides a general, facile, and unique approach for the immobilization of two oxidoreductases and gives high catalytic efficiency, long‐term and good recycling stabilities by triggering radical proton‐coupled electron transfer.

Journal

Advanced MaterialsWiley

Published: Jan 1, 2018

Keywords: ; ; ; ;

References

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