Evidence map›Paper›PMID 37168606›Full record

ArticleSynthetic and systems biotechnology2023

Engineering the thermostability of d-lyxose isomerase from

Hao Wu, Ming Yi, Xiaoyi Wu, Yating Ding, Minghui Pu, Li Wen, Yunhui Cheng, Wenli Zhang, Wanmeng Mu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Synthetic and systems biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

3 citing papers in PubMed, 19 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Hao WuSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha, 410114, China.
Ming YiSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha, 410114, China.
Xiaoyi WuSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha, 410114, China.
Yating DingSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha, 410114, China.
Minghui PuSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha, 410114, China.
Li WenSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha, 410114, China.
Yunhui ChengSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha, 410114, China.
Wenli ZhangState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, China.
Wanmeng MuState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, China.
Changsha University of Science and Technology · CNJiangnan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

d-Mannose is an attractive functional sugar that exhibits many physiological benefits on human health. The demand for low-calorie sugars and sweeteners in foods are increasingly available on the market. Some sugar isomerases, such as d-lyxose isomerase (d-LIase), can achieve an isomerization reaction between d-mannose and d-fructose. However, the weak thermostability of d-LIase limits its efficient conversion from d-fructose to d-mannose. Nonetheless, few studies are available that have investigated the molecular modification of d-LIase to improve its thermal stability. In this study, computer-aided tools including FireProt, PROSS, and Consensus Finder were employed to jointly design d-LIase mutants with improved thermostability for the first time. Finally, the obtained five-point mutant M5 (N21G/E78P/V58Y/C119Y/K170P) showed high thermal stability and catalytic activity. The half-life of M5 at 65 °C was 10.22 fold, and the catalytic efficiency towards 600 g/L of d-fructose was 2.6 times to that of the wild type enzyme, respectively. Molecular dynamics simulation and intramolecular forces analysis revealed a thermostability mechanism of highly rigidity conformation, newly formed hydrogen bonds and π-cation interaction between and within protein domains, and redistributed surface electrostatic charges for the mutant M5. This research provided a promising d-LIase mutant for the industrial production of d-mannose from d-fructose.

Indexed as

D-lyxose isomerased-mannoseMolecular modificationThermostability

Identifiers

PMID37168606
PMCPMC10165151
OpenAlexW4366607395

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.