Evidence map›Paper›PMID 40033318›Full record

ArticleMicrobial cell factories2025

Enhanced thermostability of nattokinase by rational design of disulfide bond.

Kongfang Yu, Liangqi Chen, Yaolei Tang, Aixia Ma, Wenhui Zhu, Hong Wang, Xiyu Tang, Yuan Li, Jinyao Li

Abstract read
In one paragraph

Article in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Article
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.

Kongfang Yu *Institute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China.
Liangqi Chen *Institute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China.
Yaolei TangThe Third People's Hospital of Xinjiang Uygur Autonomous Region, Urumqi, 830000, China.
Aixia MaInstitute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China.
Wenhui ZhuInstitute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China.
Hong WangInstitute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China.
Xiyu TangInstitute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China.
Yuan LiInstitute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China. liyuanstc@xju.edu.cn.
Jinyao LiInstitute of Materia Medica, College of Pharmacy, Xinjiang University, Urumqi, 830017, China. ljyxju@xju.edu.cn.

Funding

Tianchi Doctoral Program of Xinjiang Uygur Autonomous Region TCBS202124Tianshan Talent Training Program 2023TSYCLJ0043
6 · The paper itself

Abstract

Nattokinase, the thrombolytically active substance in the health food natto, nevertheless, its lower thermostability restricts its use in food and pharmaceutical applications. In this study, two heat-resistant variants of nattokinase, designated 50-109 (M1) and 15-271 (M2), were successfully obtained by introducing a disulfide bonding strategy. Their half-lives at 55℃ were found to be 2.50-fold and 5.17-fold higher, respectively, than that of the wild type. Furthermore, the specific enzyme activities of the variants, M1 and M2, were also increased by 2.37 and 1.66-fold, respectively. Meanwhile, the combination of two mutants increased the thermostability of nattokinase by 8.0-fold. Bioinformatics analyses indicated that the enhanced thermostability of the M1 and M2 variants was due to the increased rigidity and structural contraction of the overall structure. Finally, the fermentation process of mutant M1 was optimized to increase the expression of nattokinase. Study provides substantial molecular and theoretical support for the industrial production and application of nattokinase.

Indexed as

DisulfidesSubtilisinsEnzyme StabilityFermentationHot TemperatureDisulfidesnattokinaseSubtilisinsBioinformatics designDisulfide bondEnzyme synthesisNattokinaseThermostability

Identifiers

PMID40033318
PMCPMC11877946

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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.