Cargando…

A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization

Seven xylanolytic bacterial strains were isolated from saw-dust dump soil. The bacterial strain X6 was selected on the basis of the highest xylanase activity with no cellulase contamination. It was identified as Stenotrophomonas maltophilia by biochemical tests and 16S rRNA gene sequencing approach....

Descripción completa

Detalles Bibliográficos
Autores principales: Raj, Abhay, Kumar, Sharad, Singh, Sudheer Kumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3876469/
https://www.ncbi.nlm.nih.gov/pubmed/24416589
http://dx.doi.org/10.1155/2013/429305
_version_ 1782297489608540160
author Raj, Abhay
Kumar, Sharad
Singh, Sudheer Kumar
author_facet Raj, Abhay
Kumar, Sharad
Singh, Sudheer Kumar
author_sort Raj, Abhay
collection PubMed
description Seven xylanolytic bacterial strains were isolated from saw-dust dump soil. The bacterial strain X6 was selected on the basis of the highest xylanase activity with no cellulase contamination. It was identified as Stenotrophomonas maltophilia by biochemical tests and 16S rRNA gene sequencing approach. Xylanase production studies by S. maltophilia on different commercial xylans and agro-industrial residues suggested that wheat bran was the best carbon source for xylanase production (26.4 ± 0.6 IU/mL). The studies with inorganic and organic nitrogen sources suggested yeast extract as the best support for xylanase production (25 ± 0.6 IU/mL). Maximum xylanase production was observed at initial medium pH = 8.0 (23.8 ± 0.4 IU/mL) with production at pH = 7.0 and pH = 9.0 being almost comparable. Xylanase produced by S. maltophilia was purified to homogeneity using ammonium sulfate precipitation, gel filtration, and ion exchange chromatography. The final purification was 5.43-fold with recovery of 19.18%. The molecular weight of the purified xylanase protein was ~142 kDa. Both crude and purified xylanase had good stability at pH = 9.0 and 80°C with activity retention greater than 90% after 30 min incubation. The enzyme stability at high temperature and alkaline pH make it potentially effective for industrial applications.
format Online
Article
Text
id pubmed-3876469
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-38764692014-01-12 A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization Raj, Abhay Kumar, Sharad Singh, Sudheer Kumar Enzyme Res Research Article Seven xylanolytic bacterial strains were isolated from saw-dust dump soil. The bacterial strain X6 was selected on the basis of the highest xylanase activity with no cellulase contamination. It was identified as Stenotrophomonas maltophilia by biochemical tests and 16S rRNA gene sequencing approach. Xylanase production studies by S. maltophilia on different commercial xylans and agro-industrial residues suggested that wheat bran was the best carbon source for xylanase production (26.4 ± 0.6 IU/mL). The studies with inorganic and organic nitrogen sources suggested yeast extract as the best support for xylanase production (25 ± 0.6 IU/mL). Maximum xylanase production was observed at initial medium pH = 8.0 (23.8 ± 0.4 IU/mL) with production at pH = 7.0 and pH = 9.0 being almost comparable. Xylanase produced by S. maltophilia was purified to homogeneity using ammonium sulfate precipitation, gel filtration, and ion exchange chromatography. The final purification was 5.43-fold with recovery of 19.18%. The molecular weight of the purified xylanase protein was ~142 kDa. Both crude and purified xylanase had good stability at pH = 9.0 and 80°C with activity retention greater than 90% after 30 min incubation. The enzyme stability at high temperature and alkaline pH make it potentially effective for industrial applications. Hindawi Publishing Corporation 2013 2013-12-14 /pmc/articles/PMC3876469/ /pubmed/24416589 http://dx.doi.org/10.1155/2013/429305 Text en Copyright © 2013 Abhay Raj et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Raj, Abhay
Kumar, Sharad
Singh, Sudheer Kumar
A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization
title A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization
title_full A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization
title_fullStr A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization
title_full_unstemmed A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization
title_short A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization
title_sort highly thermostable xylanase from stenotrophomonas maltophilia: purification and partial characterization
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3876469/
https://www.ncbi.nlm.nih.gov/pubmed/24416589
http://dx.doi.org/10.1155/2013/429305
work_keys_str_mv AT rajabhay ahighlythermostablexylanasefromstenotrophomonasmaltophiliapurificationandpartialcharacterization
AT kumarsharad ahighlythermostablexylanasefromstenotrophomonasmaltophiliapurificationandpartialcharacterization
AT singhsudheerkumar ahighlythermostablexylanasefromstenotrophomonasmaltophiliapurificationandpartialcharacterization
AT rajabhay highlythermostablexylanasefromstenotrophomonasmaltophiliapurificationandpartialcharacterization
AT kumarsharad highlythermostablexylanasefromstenotrophomonasmaltophiliapurificationandpartialcharacterization
AT singhsudheerkumar highlythermostablexylanasefromstenotrophomonasmaltophiliapurificationandpartialcharacterization