Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process

The data presented in this article are related to the research article titled “Immobilization nd topochemical mechanism of a new β-amylase extracted from Pergularia tomentosa” (Lahmar et al., 2017) [1]. This article documented information on the determination of the molecular weight of the β-amylase...

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Autores principales: Lahmar, Imen, Radeva, Greta, Marinkova, Dessislava, Velitchkova, Maya, Belghith, Hafedh, Ben Abdallah, Ferjani, Yotova, Lyubov, Belghith, Karima
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Proteomics and Biochemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5723269/
https://www.ncbi.nlm.nih.gov/pubmed/29234697
http://dx.doi.org/10.1016/j.dib.2017.11.071
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author Lahmar, Imen
Radeva, Greta
Marinkova, Dessislava
Velitchkova, Maya
Belghith, Hafedh
Ben Abdallah, Ferjani
Yotova, Lyubov
Belghith, Karima
author_facet Lahmar, Imen
Radeva, Greta
Marinkova, Dessislava
Velitchkova, Maya
Belghith, Hafedh
Ben Abdallah, Ferjani
Yotova, Lyubov
Belghith, Karima
author_sort Lahmar, Imen
collection PubMed
description The data presented in this article are related to the research article titled “Immobilization nd topochemical mechanism of a new β-amylase extracted from Pergularia tomentosa” (Lahmar et al., 2017) [1]. This article documented information on the determination of the molecular weight of the β-amylase, the method of its immobilization and a comparison of the kinetic mechanism between the free and the immobilized forms by a mathematical method. Fresh Pergularia tomentosa was collected from Tunisia and a special method for β-amylase extraction was followed (Yotova et al., 2000) [2]. Public dissemination of this dataset will allow further analyses of the data.
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spelling pubmed-57232692017-12-11 Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process Lahmar, Imen Radeva, Greta Marinkova, Dessislava Velitchkova, Maya Belghith, Hafedh Ben Abdallah, Ferjani Yotova, Lyubov Belghith, Karima Data Brief Proteomics and Biochemistry The data presented in this article are related to the research article titled “Immobilization nd topochemical mechanism of a new β-amylase extracted from Pergularia tomentosa” (Lahmar et al., 2017) [1]. This article documented information on the determination of the molecular weight of the β-amylase, the method of its immobilization and a comparison of the kinetic mechanism between the free and the immobilized forms by a mathematical method. Fresh Pergularia tomentosa was collected from Tunisia and a special method for β-amylase extraction was followed (Yotova et al., 2000) [2]. Public dissemination of this dataset will allow further analyses of the data. Elsevier 2017-11-23 /pmc/articles/PMC5723269/ /pubmed/29234697 http://dx.doi.org/10.1016/j.dib.2017.11.071 Text en © 2017 The Authors 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
Lahmar, Imen
Radeva, Greta
Marinkova, Dessislava
Velitchkova, Maya
Belghith, Hafedh
Ben Abdallah, Ferjani
Yotova, Lyubov
Belghith, Karima
Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process
title Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process
title_full Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process
title_fullStr Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process
title_full_unstemmed Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process
title_short Valorization of a plant β-amylase: Immobilization and dataset on the kinetic process
title_sort valorization of a plant β-amylase: immobilization and dataset on the kinetic process
topic Proteomics and Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5723269/
https://www.ncbi.nlm.nih.gov/pubmed/29234697
http://dx.doi.org/10.1016/j.dib.2017.11.071
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