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Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8

Thermomyces lanuginosus SS-8 was isolated from soil samples that had been collected from near self-heating plant material and its extracellular cellulase-free xylanase purified approximately 160-fold using ion exchange chromatography and continuous elution electrophoresis. This xylanase was thermoac...

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Autores principales: Shrivastava, Smriti, Shukla, Pratyoosh, Mukhopadhyay, Kunal
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339585/
https://www.ncbi.nlm.nih.gov/pubmed/22558544
http://dx.doi.org/10.1007/s13205-011-0032-6
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author Shrivastava, Smriti
Shukla, Pratyoosh
Mukhopadhyay, Kunal
author_facet Shrivastava, Smriti
Shukla, Pratyoosh
Mukhopadhyay, Kunal
author_sort Shrivastava, Smriti
collection PubMed
description Thermomyces lanuginosus SS-8 was isolated from soil samples that had been collected from near self-heating plant material and its extracellular cellulase-free xylanase purified approximately 160-fold using ion exchange chromatography and continuous elution electrophoresis. This xylanase was thermoactive (optimum temperature 60 °C) at pH 6.0 and had a molecular weight of 23.79 kDa as indicated by SDS-PAGE electrophoresis. The xylanase rapidly hydrolyzed xylan directly to xylose without the production of intermediary xylo-oligosaccharides within 15 min of incubation under optimum conditions. This trait of rapidly degrading xylan to xylose as a sole end-product could have biotechnological potential in degradation of agro-wastes for bioethanol manufacturing industry.
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spelling pubmed-33395852012-05-01 Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8 Shrivastava, Smriti Shukla, Pratyoosh Mukhopadhyay, Kunal 3 Biotech Original Article Thermomyces lanuginosus SS-8 was isolated from soil samples that had been collected from near self-heating plant material and its extracellular cellulase-free xylanase purified approximately 160-fold using ion exchange chromatography and continuous elution electrophoresis. This xylanase was thermoactive (optimum temperature 60 °C) at pH 6.0 and had a molecular weight of 23.79 kDa as indicated by SDS-PAGE electrophoresis. The xylanase rapidly hydrolyzed xylan directly to xylose without the production of intermediary xylo-oligosaccharides within 15 min of incubation under optimum conditions. This trait of rapidly degrading xylan to xylose as a sole end-product could have biotechnological potential in degradation of agro-wastes for bioethanol manufacturing industry. Springer Berlin Heidelberg 2011-10-22 2011-12 /pmc/articles/PMC3339585/ /pubmed/22558544 http://dx.doi.org/10.1007/s13205-011-0032-6 Text en © The Author(s) 2011 https://creativecommons.org/licenses/by/4.0/ This article is published under license to BioMed Central Ltd. Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Original Article
Shrivastava, Smriti
Shukla, Pratyoosh
Mukhopadhyay, Kunal
Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8
title Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8
title_full Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8
title_fullStr Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8
title_full_unstemmed Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8
title_short Purification and preliminary characterization of a xylanase from Thermomyces lanuginosus strain SS-8
title_sort purification and preliminary characterization of a xylanase from thermomyces lanuginosus strain ss-8
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3339585/
https://www.ncbi.nlm.nih.gov/pubmed/22558544
http://dx.doi.org/10.1007/s13205-011-0032-6
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