Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris

Glucose Oxidase (GOD), is a common flavoprotein from Aspergillus niger ATCC 9029 with a broad application in biotechnology, food and medical industries. In this study, GOD gene was cloned into the expression vector, pPIC9 and screened by the alcohol oxidase promoter. The enzyme production increased...

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Autores principales: Belyad, Fakhry, Karkhanei, Ali Asghar, Raheb, Jamshid
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6126455/
https://www.ncbi.nlm.nih.gov/pubmed/30197862
http://dx.doi.org/10.1016/j.euprot.2018.09.001
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author Belyad, Fakhry
Karkhanei, Ali Asghar
Raheb, Jamshid
author_facet Belyad, Fakhry
Karkhanei, Ali Asghar
Raheb, Jamshid
author_sort Belyad, Fakhry
collection PubMed
description Glucose Oxidase (GOD), is a common flavoprotein from Aspergillus niger ATCC 9029 with a broad application in biotechnology, food and medical industries. In this study, GOD gene was cloned into the expression vector, pPIC9 and screened by the alcohol oxidase promoter. The enzyme production increased at 28 °C. GOD activity induced by 1.0% methanol and the highest level of GOD production was the result of shaking rate at 225 rpm. The highest enzyme activity obtained at a pH value ranged from 5 to 7 at 50 °C. The enzyme was stable at a broad pH range and temperature.
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spelling pubmed-61264552018-09-07 Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris Belyad, Fakhry Karkhanei, Ali Asghar Raheb, Jamshid EuPA Open Proteom Article Glucose Oxidase (GOD), is a common flavoprotein from Aspergillus niger ATCC 9029 with a broad application in biotechnology, food and medical industries. In this study, GOD gene was cloned into the expression vector, pPIC9 and screened by the alcohol oxidase promoter. The enzyme production increased at 28 °C. GOD activity induced by 1.0% methanol and the highest level of GOD production was the result of shaking rate at 225 rpm. The highest enzyme activity obtained at a pH value ranged from 5 to 7 at 50 °C. The enzyme was stable at a broad pH range and temperature. Elsevier 2018-09-03 /pmc/articles/PMC6126455/ /pubmed/30197862 http://dx.doi.org/10.1016/j.euprot.2018.09.001 Text en © 2018 Published by Elsevier B.V. on behalf of European Proteomics Association (EuPA). http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Article
Belyad, Fakhry
Karkhanei, Ali Asghar
Raheb, Jamshid
Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
title Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
title_full Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
title_fullStr Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
title_full_unstemmed Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
title_short Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris
title_sort expression, characterization and one step purification of heterologous glucose oxidase gene from aspergillus niger atcc 9029 in pichia pastoris
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6126455/
https://www.ncbi.nlm.nih.gov/pubmed/30197862
http://dx.doi.org/10.1016/j.euprot.2018.09.001
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