Evidence map›Paper›PMID 30236091›Full record

ArticleBMC biotechnology2018

Consensus design for improved thermostability of lipoxygenase from Anabaena sp. PCC 7120.

Hui Qian, Chong Zhang, Zhaoxin Lu, Bingjie Xia, Xiaomei Bie, Haizhen Zhao, Fengxia Lu, Guang-Yu Yang

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

10 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Improved catalytic performance and molecular insight for lipoxygenase fromFrontiers in bioengineering and biotechnology · 2023
    Article
  8. Thermostability Improvement of L-Asparaginase fromMolecules (Basel, Switzerland) · 2022
    Article
  9. Article
  10. 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

8 authors at 2 institutions in 1 country.

Hui QianCollege of Food Science and Technology, Nanjing Agricultural University, 1st Weigang, Nanjing, 210095, People's Republic of China.
Chong ZhangCollege of Food Science and Technology, Nanjing Agricultural University, 1st Weigang, Nanjing, 210095, People's Republic of China.
Zhaoxin LuCollege of Food Science and Technology, Nanjing Agricultural University, 1st Weigang, Nanjing, 210095, People's Republic of China.
Bingjie XiaCollege of Food Science and Technology, Nanjing Agricultural University, 1st Weigang, Nanjing, 210095, People's Republic of China.
Xiaomei BieCollege of Food Science and Technology, Nanjing Agricultural University, 1st Weigang, Nanjing, 210095, People's Republic of China.
Haizhen ZhaoCollege of Food Science and Technology, Nanjing Agricultural University, 1st Weigang, Nanjing, 210095, People's Republic of China.
Fengxia LuCollege of Food Science and Technology, Nanjing Agricultural University, 1st Weigang, Nanjing, 210095, People's Republic of China. lufengxia@njau.edu.cn.
Guang-Yu YangState Key Laboratory of Microbial Metabolism, College of Life Science and Biotechnology, Shanghai Jiao Tong University, 800 Dongchuan Rd, Shanghai, 200240, People's Republic of China. yanggy@sjtu.edu.cn.
Nanjing Agricultural University · CNShanghai Jiao Tong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundLipoxygenase (LOX) from Anabaena sp. PCC 7120 (Ana-rLOX) offers important applications in the food industry, especially for improving aroma and dough rheological properties. However, industrial applications of LOXs have been limited by their poor thermostability. Herein, we report a bioinformatics-based consensus concept approach for the engineering of thermostable Ana-rLOX.

resultsA series of mutations (N130D, G260A, S437T, N130D/G260Q, N130D/S437Y) showed higher thermostability and activity than the wild-type enzyme. Thus, N130D/G260Q exhibited a 6.6-fold increase in half-life and 2.45 °C increase in unfolding temperature; N130D/S437Y showed a 10 °C increase in optimal temperature. The secondary structure did not change much that contributed to improved thermostability were investigated in detail using circular dichroism. Homology modeling suggested that enhanced thermostability and specific activity may result from favorable hydrophobic interactions.

conclusionsA series of mutations were achieved, showing higher thermostability and activity than the wild-type enzyme by semi-rational mutagenesis with limited structure information. Our findings provide important new insights into molecular modifications aimed at improving Ana-rLOX thermostability and activity.

Indexed as

AnabaenaBacterial ProteinsCircular DichroismEnzyme StabilityKineticsLipoxygenaseMutagenesis, Site-DirectedProtein EngineeringTemperatureBacterial ProteinsLipoxygenaseConsensus conceptLipoxygenaseSpecific activityThermostability

Identifiers

PMID30236091
PMCPMC6148764
OpenAlexW2890913936

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.