Evidence map›Paper›PMID 39614912›Full record

ArticleBiotechnology letters2024

Characterization, immobilization and evaluation of anti-Pseudomonas aeruginosa biofilm activity of alginate lyase from marine bacterium, Enterobacter tabaci RAU2C.

Ramya Petchimuthu, Krishnan Sundar, Vanavil Balakrishnan

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Article in Biotechnology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Ramya PetchimuthuDepartment of Biotechnology, Kalasalingam Academy of Research and Education, Krishnankoil, Tamil Nadu, 626 126, India.
Krishnan SundarDepartment of Biotechnology, Kalasalingam Academy of Research and Education, Krishnankoil, Tamil Nadu, 626 126, India.
Vanavil BalakrishnanDepartment of Biotechnology, Kalasalingam Academy of Research and Education, Krishnankoil, Tamil Nadu, 626 126, India. b.vanavil@klu.ac.in.ORCID http://orcid.org/0000-0002-5687-0588

Funding

Kalasalingam Academy of Research and Education KARE/VC/R&D/SMPG/2023-2024/01
6 · The paper itself

Abstract

Alginate lyases have the potential to be used as a therapeutic agent for P. aeruginosa infections. The present work was focused on the characterization of free and immobilized alginate lyase produced by marine bacteria, Enterobacter tabaci RAU2C isolated previously in the laboratory for alginate lyase production and exploring the potential of alginate lyase as an anti-biofilm agent against the P. aeruginosa biofilm. RAU2C alginate lyase was immobilized using an epoxy-activated curdlan matrix by three different methods. Further, the free and immobilized were characterized for its optimal pH and temperature. The effect of alginate concentration on alginate lyase activity was assessed and the kinetic parameters were evaluated. The anti-biofilm activity of the crude alginate lyase was studied using biofilm inhibition and disruption assays in microtiter plates with crystal violet. The biofilm disruption by RAU2C alginate lyase was also ascertained by microscopic analysis. The immobilization matrix prepared using method 3 had a better binding capacity compared to other methods. Both soluble and immobilized alginate lyase exhibited optimal activity at 37 °C and pH 7.0. K

Indexed as

Anti-Bacterial AgentsBiofilmsEnterobacterEnzymes, ImmobilizedPolysaccharide-LyasesPseudomonas aeruginosaAlginatesEnzyme StabilityHydrogen-Ion ConcentrationKineticsTemperatureAlginatesAnti-Bacterial AgentsEnzymes, Immobilizedpoly(beta-D-mannuronate) lyasePolysaccharide-LyasesAlginate lyaseBiofilmEnzyme drugsImmobilizationMarine bacteriaPseudomonas aeruginosa

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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.