Evidence map›Paper›PMID 31079316›Full record

ArticleMolecular biology reports2019

Characterization of recombinant endo-1,4-β-xylanase of Bacillus halodurans C-125 and rational identification of hot spot amino acid residues responsible for enhancing thermostability by an in-silico approach.

Malik Siddique Mahmood, Faiz Rasul, Mahjabeen Saleem, Amber Afroz, Muhammad Faheem Malik, Naeem Mehmood Ashraf, Umar Rashid, Shumaila Naz, Nadia Zeeshan

Abstract read
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Article in Molecular biology reports, 2019. 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
0.7field-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

3 citing papers in PubMed, 11 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 3 institutions in 2 countries.

Malik Siddique MahmoodInstitute of Biochemistry and Biotechnology, University of the Punjab, P. O Box No, 54590, Lahore, Pakistan.
Faiz RasulDepartment of Biochemistry and Molecular Biology, University of Science and Technology, Hefei, China.
Mahjabeen SaleemInstitute of Biochemistry and Biotechnology, University of the Punjab, P. O Box No, 54590, Lahore, Pakistan.
Amber AfrozDepartment of Biochemistry and Biotechnology, University of Gujrat, P. O Box No. 50700, Gujrat, Pakistan.
Muhammad Faheem MalikDepartment of Biochemistry and Biotechnology, University of Gujrat, P. O Box No. 50700, Gujrat, Pakistan.
Naeem Mehmood AshrafDepartment of Biochemistry and Biotechnology, University of Gujrat, P. O Box No. 50700, Gujrat, Pakistan.
Umar RashidDepartment of Biochemistry and Biotechnology, University of Gujrat, P. O Box No. 50700, Gujrat, Pakistan.
Shumaila NazDepartment of Biosciences, University of Gujrat, Gujrat, Pakistan.
Nadia ZeeshanDepartment of Biochemistry and Biotechnology, University of Gujrat, P. O Box No. 50700, Gujrat, Pakistan. nadia.zeeshan@uog.edu.pk.ORCID http://orcid.org/0000-0003-0701-7078
University of Gujrat · PKUniversity of the Punjab · PKUniversity of Science and Technology of China · CN

Funding

Higher Education Commission (HEC), Pakistan PM-IPFP/HRD/HEC/2011/0018Higher Education commission, Pakistan Ph D Fellowship 5000 Phase II" Award No. 315-2158-2BS3-029.
6 · The paper itself

Abstract

Increased demand of enzymes for industrial use has led the scientists towards protein engineering techniques. In different protein engineering strategies, rational approach has emerged as the most efficient method utilizing bioinformatics tools to produce enzymes with desired reaction kinetics; physiochemical (temperature, pH, half life, etc) and biological (selectivity, specificity, etc.) characteristics. Xylanase is one of the widely used enzymes in paper and food industry to degrade xylan component present in plant pulp. In this study endo 1,4-β-xylanase (Xyl-11A) from Bacillus halodurans C-125 was cloned in pET-22b (+) vector and expressed in Escherichia coli BL21 (DE3) expression strain. The enzyme had Michaelis constant K

Indexed as

Amino AcidsBacillusBase SequenceCloning, MolecularComputer SimulationEndo-1,4-beta XylanasesEnzyme StabilityKineticsModels, MolecularMutant ProteinsProtein EngineeringRecombinant ProteinsTemperatureAmino AcidsEndo-1,4-beta XylanasesMutant ProteinsRecombinant ProteinsBacillus halodurans C-125Cloning and expressionComputational rational designEndo 1,4-β-xylanaseThermostabilityXylanase

Identifiers

PMID31079316
OpenAlexW2943950151

What Socratic 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 Socratic graph.