Evidence map›Paper›PMID 35771268›Full record

ArticleBioprocess and biosystems engineering2022

Biodegradation of anionic polyacrylamide by manganese peroxidase: docking, virtual mutation based on affinity, QM/MM calculation and molecular dynamics simulation.

Fanglue Wang, Dongchen Zhang, Liwen Zhang, Xuefeng Wu, Shengsong Deng, Xinyu Yuan

Abstract read
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In one paragraph

Article in Bioprocess and biosystems engineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. 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

6 authors at 3 institutions in 1 country.

Fanglue WangSchool of Material Science and Engineering, Anhui University of Science and Technology, Huainan, 232001, China. wangfanglue66@163.com.ORCID http://orcid.org/0000-0002-1795-4543
Dongchen ZhangSchool of Material Science and Engineering, Anhui University of Science and Technology, Huainan, 232001, China.
Liwen ZhangSchool of Mechanical and Electrical Engineering, Huainan Normal University, Huainan, 232001, China.
Xuefeng WuSchool of Food and Bioengineering, Hefei University of Technology, Hefei, 230009, China.
Shengsong DengSchool of Food and Bioengineering, Hefei University of Technology, Hefei, 230009, China.
Xinyu YuanSchool of Food and Bioengineering, Hefei University of Technology, Hefei, 230009, China.
Hefei University of Technology · CNAnhui University of Science and Technology · CNHuainan Normal University · CN

Funding

National Natural Science Foundation of China 31601465National Natural Science Foundation of China 51274012
6 · The paper itself

Abstract

Manganese peroxidase (Mn P) is capable of effectively degrading anionic polyacrylamide (HPAM). However, the interaction of Mn P with HPAM at molecular level is lacking until now. Here, the HPAM model compounds, HPAM-2, HPAM-3, HPAM-4, and HPAM-5, were selected to reveal their binding mechanisms with Mn P. The results showed that the most suitable substrate for Mn P was HPAM-5, and the main reason for MnP-HPAM-5 with maximal affinity was strong hydrogen bond. LYS96 was the important key residue in all complexes, and the number of key residue was largest in MnP-HPAM-5. The optimal THR27ILE mutant may enhance the affinity of Mn P to HPAM-4. The stability of Mn P binding to HPAM-4 was the optimal. These results were helpful in designing highly efficient Mn P against HPAM to protect the ecological environment.

Indexed as

Molecular Dynamics SimulationPeroxidasesAcrylic ResinsBiodegradation, EnvironmentalMutationPolyacrylamidesAcrylic Resinsmanganese peroxidasePeroxidasesPolyacrylamidesAnionic polyacrylamide (HPAM)Ecological environmentEnzyme structureManganese peroxidase (Mn P)

Identifiers

PMID35771268
OpenAlexW4283758093

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.