PMID- 37452834
OWN - NLM
STAT- MEDLINE
DCOM- 20230808
LR  - 20230808
IS  - 1615-7605 (Electronic)
IS  - 1615-7591 (Linking)
VI  - 46
IP  - 9
DP  - 2023 Sep
TI  - Construction of metal-organic framework-based multienzyme system for 
      L-tert-leucine production.
PG  - 1365-1373
LID - 10.1007/s00449-023-02900-6 [doi]
AB  - Chiral compounds are important drug intermediates that play a critical role in 
      human life. Herein, we report a facile method to prepare multi-enzyme 
      nano-devices with high catalytic activity and stability. The self-assemble 
      molecular binders SpyCatcher and SpyTag were fused with leucine dehydrogenase and 
      glucose dehydrogenase to produce sc-LeuDH (SpyCatcher-fused leucine 
      dehydrogenase) and GDH-st (SpyTag-fused glucose dehydrogenase), respectively. 
      After assembling, the cross-linked enzymes LeuDH-GDH were formed. The 
      crosslinking enzyme has good pH stability and temperature stability. The coenzyme 
      cycle constant of LeuDH-GDH was always higher than that of free double enzymes. 
      The yield of L-tert-leucine synthesis by LeuDH-GDH was 0.47 times higher than 
      that by free LeuDH and GDH. To further improve the enzyme performance, the 
      cross-linked LeuDH-GDH was immobilized on zeolite imidazolate framework-8 (ZIF-8) 
      via bionic mineralization, forming LeuDH-GDH @ZIF-8. The created co-immobilized 
      enzymes showed even better pH stability and temperature stability than the 
      cross-linked enzymes, and LeuDH-GDH@ZIF-8 retains 70% relative conversion rate in 
      the first four reuses. In addition, the yield of LeuDH-GDH@ZIF-8 was 0.62 times 
      higher than that of LeuDH-GDH, and 1.38 times higher than that of free double 
      enzyme system. This work provides a novel method for developing multi-enzyme 
      nano-device, and the ease of operation of this method is appealing for the 
      construction of other multi-enzymes @MOF systems for the applications in the 
      kinds of complex environment.
CI  - (c) 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, 
      part of Springer Nature.
FAU - Wang, Ru
AU  - Wang R
AD  - School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, 
      Nanjing, 210046, China.
FAU - Jia, Jianyao
AU  - Jia J
AD  - School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, 
      Nanjing, 210046, China.
FAU - Liu, Xue
AU  - Liu X
AD  - School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, 
      Nanjing, 210046, China.
FAU - Chen, Yaru
AU  - Chen Y
AD  - School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, 
      Nanjing, 210046, China.
FAU - Xu, Qing
AU  - Xu Q
AD  - School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, 
      Nanjing, 210046, China. xu_qing@njnu.edu.cn.
FAU - Xue, Feng
AU  - Xue F
AD  - School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, 
      Nanjing, 210046, China. xuef2020@njnu.edu.cn.
LA  - eng
GR  - 2021M691624/China Postdoctoral Science Foundation/
GR  - 21878154/National Natural Science Foundation of China/
PT  - Journal Article
DEP - 20230715
PL  - Germany
TA  - Bioprocess Biosyst Eng
JT  - Bioprocess and biosystems engineering
JID - 101088505
RN  - EC 1.4.1.9 (Leucine Dehydrogenase)
RN  - 0 (Metal-Organic Frameworks)
RN  - 471-50-1 (2-amino-3,3-dimethylbutanoic acid)
RN  - GMW67QNF9C (Leucine)
RN  - EC 1.1.1.- (Glucose Dehydrogenases)
SB  - IM
EIN - Bioprocess Biosyst Eng. 2023 Aug 2;:. PMID: 37528274
MH  - Humans
MH  - Leucine Dehydrogenase/chemistry
MH  - *Metal-Organic Frameworks
MH  - Leucine/chemistry
MH  - Glucose Dehydrogenases
OTO - NOTNLM
OT  - Glucose dehydrogenase
OT  - L-tert-Leucine
OT  - Leucine dehydrogenase
OT  - Metal-organic framework
OT  - Protein crosslinking
EDAT- 2023/07/15 21:05
MHDA- 2023/08/08 06:42
CRDT- 2023/07/15 11:03
PHST- 2023/03/16 00:00 [received]
PHST- 2023/06/22 00:00 [accepted]
PHST- 2023/08/08 06:42 [medline]
PHST- 2023/07/15 21:05 [pubmed]
PHST- 2023/07/15 11:03 [entrez]
AID - 10.1007/s00449-023-02900-6 [pii]
AID - 10.1007/s00449-023-02900-6 [doi]
PST - ppublish
SO  - Bioprocess Biosyst Eng. 2023 Sep;46(9):1365-1373. doi: 
      10.1007/s00449-023-02900-6. Epub 2023 Jul 15.