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Purification of an Inducible DNase from a Thermophilic Fungus

The ability to induce an extracellular DNase from a novel thermophilic fungus was studied and the DNAse purified using both traditional and innovative purification techniques. The isolate produced sterile hyphae under all attempted growing conditions, with an average diameter of 2 μm and was found t...

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Detalles Bibliográficos
Autores principales: Landry, Kyle S., Vu, Andrea, Levin, Robert E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907870/
https://www.ncbi.nlm.nih.gov/pubmed/24447923
http://dx.doi.org/10.3390/ijms15011300
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author Landry, Kyle S.
Vu, Andrea
Levin, Robert E.
author_facet Landry, Kyle S.
Vu, Andrea
Levin, Robert E.
author_sort Landry, Kyle S.
collection PubMed
description The ability to induce an extracellular DNase from a novel thermophilic fungus was studied and the DNAse purified using both traditional and innovative purification techniques. The isolate produced sterile hyphae under all attempted growing conditions, with an average diameter of 2 μm and was found to have an optimal temperature of 45 °C and a maximum of 65 °C. Sequencing of the internal transcribed region resulted in a 91% match with Chaetomium sp., suggesting a new species, but further clarification on this point is needed. The optimal temperature for DNase production was found to be 55 °C and was induced by the presence of DNA and/or deoxyribose. Static growth of the organism resulted in significantly higher DNase production than agitated growth. The DNase was purified 145-fold using a novel affinity membrane purification system with 25% of the initial enzyme activity remaining. Electrophoresis of the purified enzyme resulted in a single protein band, indicating DNase homogeneity.
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spelling pubmed-39078702014-01-31 Purification of an Inducible DNase from a Thermophilic Fungus Landry, Kyle S. Vu, Andrea Levin, Robert E. Int J Mol Sci Article The ability to induce an extracellular DNase from a novel thermophilic fungus was studied and the DNAse purified using both traditional and innovative purification techniques. The isolate produced sterile hyphae under all attempted growing conditions, with an average diameter of 2 μm and was found to have an optimal temperature of 45 °C and a maximum of 65 °C. Sequencing of the internal transcribed region resulted in a 91% match with Chaetomium sp., suggesting a new species, but further clarification on this point is needed. The optimal temperature for DNase production was found to be 55 °C and was induced by the presence of DNA and/or deoxyribose. Static growth of the organism resulted in significantly higher DNase production than agitated growth. The DNase was purified 145-fold using a novel affinity membrane purification system with 25% of the initial enzyme activity remaining. Electrophoresis of the purified enzyme resulted in a single protein band, indicating DNase homogeneity. Molecular Diversity Preservation International (MDPI) 2014-01-20 /pmc/articles/PMC3907870/ /pubmed/24447923 http://dx.doi.org/10.3390/ijms15011300 Text en © 2014 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Landry, Kyle S.
Vu, Andrea
Levin, Robert E.
Purification of an Inducible DNase from a Thermophilic Fungus
title Purification of an Inducible DNase from a Thermophilic Fungus
title_full Purification of an Inducible DNase from a Thermophilic Fungus
title_fullStr Purification of an Inducible DNase from a Thermophilic Fungus
title_full_unstemmed Purification of an Inducible DNase from a Thermophilic Fungus
title_short Purification of an Inducible DNase from a Thermophilic Fungus
title_sort purification of an inducible dnase from a thermophilic fungus
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907870/
https://www.ncbi.nlm.nih.gov/pubmed/24447923
http://dx.doi.org/10.3390/ijms15011300
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