Evidence map›Paper›PMID 37452834›Full record

ArticleBioprocess and biosystems engineering2023

Construction of metal-organic framework-based multienzyme system for L-tert-leucine production.

Ru Wang, Jianyao Jia, Xue Liu, Yaru Chen, Qing Xu, Feng Xue

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Bioprocess and biosystems engineering, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Ru WangSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210046, China.
Jianyao JiaSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210046, China.
Xue LiuSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210046, China.
Yaru ChenSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210046, China.
Qing XuSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210046, China. xu_qing@njnu.edu.cn.
Feng XueSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210046, China. xuef2020@njnu.edu.cn.
Nanjing Normal University · CN

Funding

China Postdoctoral Science Foundation 2021M691624National Natural Science Foundation of China 21878154
6 · The paper itself

Abstract

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.

Indexed as

Metal-Organic FrameworksGlucose DehydrogenasesHumansLeucineLeucine Dehydrogenase2-amino-3,3-dimethylbutanoic acidGlucose DehydrogenasesLeucineLeucine DehydrogenaseMetal-Organic FrameworksGlucose dehydrogenaseLeucine dehydrogenaseL-tert-LeucineMetal–organic frameworkProtein crosslinking

Identifiers

PMID37452834
OpenAlexW4384405788

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.