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l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene
Marine actinobacteria are known to be a rich source for novel metabolites with diverse biological activities. In this study, a potential extracellular L-asparaginase was characterised from the Streptomyces griseus NIOT-VKMA29. Box-Behnken based optimization was used to determine the culture medium c...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4513294/ https://www.ncbi.nlm.nih.gov/pubmed/26206135 http://dx.doi.org/10.1038/srep12404 |
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author | Meena, Balakrishnan Anburajan, Lawrance Sathish, Thadikamala Vijaya Raghavan, Rangamaran Dharani, Gopal Valsalan Vinithkumar, Nambali Kirubagaran, Ramalingam |
author_facet | Meena, Balakrishnan Anburajan, Lawrance Sathish, Thadikamala Vijaya Raghavan, Rangamaran Dharani, Gopal Valsalan Vinithkumar, Nambali Kirubagaran, Ramalingam |
author_sort | Meena, Balakrishnan |
collection | PubMed |
description | Marine actinobacteria are known to be a rich source for novel metabolites with diverse biological activities. In this study, a potential extracellular L-asparaginase was characterised from the Streptomyces griseus NIOT-VKMA29. Box-Behnken based optimization was used to determine the culture medium components to enhance the L-asparaginase production. pH, starch, yeast extract and L-asparagine has a direct correlation for enzyme production with a maximum yield of 56.78 IU mL(−1). A verification experiment was performed to validate the experiment and more than 99% validity was established. L-Asparaginase biosynthesis gene (ansA) from Streptomyces griseus NIOT-VKMA29 was heterologously expressed in Escherichia coli M15 and the enzyme production was increased threefold (123 IU mL(−1)) over the native strain. The ansA gene sequences reported in this study encloses several base substitutions with that of reported sequences in GenBank, resulting in altered amino acid sequences of the translated protein. |
format | Online Article Text |
id | pubmed-4513294 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-45132942015-07-29 l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene Meena, Balakrishnan Anburajan, Lawrance Sathish, Thadikamala Vijaya Raghavan, Rangamaran Dharani, Gopal Valsalan Vinithkumar, Nambali Kirubagaran, Ramalingam Sci Rep Article Marine actinobacteria are known to be a rich source for novel metabolites with diverse biological activities. In this study, a potential extracellular L-asparaginase was characterised from the Streptomyces griseus NIOT-VKMA29. Box-Behnken based optimization was used to determine the culture medium components to enhance the L-asparaginase production. pH, starch, yeast extract and L-asparagine has a direct correlation for enzyme production with a maximum yield of 56.78 IU mL(−1). A verification experiment was performed to validate the experiment and more than 99% validity was established. L-Asparaginase biosynthesis gene (ansA) from Streptomyces griseus NIOT-VKMA29 was heterologously expressed in Escherichia coli M15 and the enzyme production was increased threefold (123 IU mL(−1)) over the native strain. The ansA gene sequences reported in this study encloses several base substitutions with that of reported sequences in GenBank, resulting in altered amino acid sequences of the translated protein. Nature Publishing Group 2015-07-24 /pmc/articles/PMC4513294/ /pubmed/26206135 http://dx.doi.org/10.1038/srep12404 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Meena, Balakrishnan Anburajan, Lawrance Sathish, Thadikamala Vijaya Raghavan, Rangamaran Dharani, Gopal Valsalan Vinithkumar, Nambali Kirubagaran, Ramalingam l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene |
title | l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene |
title_full | l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene |
title_fullStr | l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene |
title_full_unstemmed | l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene |
title_short | l-Asparaginase from Streptomyces griseus NIOT-VKMA29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene |
title_sort | l-asparaginase from streptomyces griseus niot-vkma29: optimization of process variables using factorial designs and molecular characterization of l-asparaginase gene |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4513294/ https://www.ncbi.nlm.nih.gov/pubmed/26206135 http://dx.doi.org/10.1038/srep12404 |
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