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Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium

Bacillus lehensis G1 is a cyclodextrin glucanotransferase (CGTase) producer, which can degrade starch into cyclodextrin. Here, we present the proteomics data of B. lehensis cultured in starch-containing medium, which is related to the article “Proteome-based identification of signal peptides for imp...

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Detalles Bibliográficos
Autores principales: Ling, How Lie, Rahmat, Zaidah, Murad, Abdul Munir Abdul, Mahadi, Nor Muhammad, Illias, Rosli Md.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5524313/
https://www.ncbi.nlm.nih.gov/pubmed/28761915
http://dx.doi.org/10.1016/j.dib.2017.07.026
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author Ling, How Lie
Rahmat, Zaidah
Murad, Abdul Munir Abdul
Mahadi, Nor Muhammad
Illias, Rosli Md.
author_facet Ling, How Lie
Rahmat, Zaidah
Murad, Abdul Munir Abdul
Mahadi, Nor Muhammad
Illias, Rosli Md.
author_sort Ling, How Lie
collection PubMed
description Bacillus lehensis G1 is a cyclodextrin glucanotransferase (CGTase) producer, which can degrade starch into cyclodextrin. Here, we present the proteomics data of B. lehensis cultured in starch-containing medium, which is related to the article “Proteome-based identification of signal peptides for improved secretion of recombinant cyclomaltodextrin glucanotransferase in Escherichia coli” (Ling et. al, in press). This dataset was generated to better understand the secretion of proteins involved in starch utilization for bacterial sustained growth. A 2-DE proteomic technique was used and the proteins were tryptically digested followed by detection using MALDI-TOF/TOF. Proteins were classified into functional groups using the information available in SubtiList webserver (http://genolist.pasteur.fr/SubtiList/).
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spelling pubmed-55243132017-07-31 Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium Ling, How Lie Rahmat, Zaidah Murad, Abdul Munir Abdul Mahadi, Nor Muhammad Illias, Rosli Md. Data Brief Proteomics and Biochemistry Bacillus lehensis G1 is a cyclodextrin glucanotransferase (CGTase) producer, which can degrade starch into cyclodextrin. Here, we present the proteomics data of B. lehensis cultured in starch-containing medium, which is related to the article “Proteome-based identification of signal peptides for improved secretion of recombinant cyclomaltodextrin glucanotransferase in Escherichia coli” (Ling et. al, in press). This dataset was generated to better understand the secretion of proteins involved in starch utilization for bacterial sustained growth. A 2-DE proteomic technique was used and the proteins were tryptically digested followed by detection using MALDI-TOF/TOF. Proteins were classified into functional groups using the information available in SubtiList webserver (http://genolist.pasteur.fr/SubtiList/). Elsevier 2017-07-14 /pmc/articles/PMC5524313/ /pubmed/28761915 http://dx.doi.org/10.1016/j.dib.2017.07.026 Text en © 2017 Published by Elsevier Inc. http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Proteomics and Biochemistry
Ling, How Lie
Rahmat, Zaidah
Murad, Abdul Munir Abdul
Mahadi, Nor Muhammad
Illias, Rosli Md.
Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium
title Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium
title_full Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium
title_fullStr Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium
title_full_unstemmed Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium
title_short Data for proteome analysis of Bacillus lehensis G1 in starch-containing medium
title_sort data for proteome analysis of bacillus lehensis g1 in starch-containing medium
topic Proteomics and Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5524313/
https://www.ncbi.nlm.nih.gov/pubmed/28761915
http://dx.doi.org/10.1016/j.dib.2017.07.026
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