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Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization

Bacterial cellulose spheres subjected to amination and inlaid modification with superparamagnetic molecules were analyzed with regard to possibility of their application as an immobilization carrier of Lecitase® Ultra (LU) enzyme. The starting point to obtain the carrier was synthesis of bacterial c...

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Autores principales: Drozd, Radosław, Szymańska, Magdalena, Rakoczy, Rafał, Junka, Adam, Szymczyk, Patrycja, Fijałkowski, Karol
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6326999/
https://www.ncbi.nlm.nih.gov/pubmed/29911267
http://dx.doi.org/10.1007/s12010-018-2816-1
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author Drozd, Radosław
Szymańska, Magdalena
Rakoczy, Rafał
Junka, Adam
Szymczyk, Patrycja
Fijałkowski, Karol
author_facet Drozd, Radosław
Szymańska, Magdalena
Rakoczy, Rafał
Junka, Adam
Szymczyk, Patrycja
Fijałkowski, Karol
author_sort Drozd, Radosław
collection PubMed
description Bacterial cellulose spheres subjected to amination and inlaid modification with superparamagnetic molecules were analyzed with regard to possibility of their application as an immobilization carrier of Lecitase® Ultra (LU) enzyme. The starting point to obtain the carrier was synthesis of bacterial cellulose spheres performed in shaking cultures of Komagataeibacter xylinus. These spheres were subsequently subjected to a multi-stage modification to increase the efficiency of the immobilization process and to separate product from the reaction medium. Maximal yield of Lecitase® Ultra immobilization equaled 70%. It was also found that immobilization process did not affect the pH and LU temperature optimum. Moreover, immobilized enzyme exhibited similar temperature stability profile as its native form. The immobilization process did not significantly affect the enzyme K(M) value. The immobilized enzyme retained over 70% of its initial activity after 8 cycles of use. The immobilized enzyme displayed good storage stability and retained 80% of its initial activity after 4 weeks at 4 °C. The potential application of such modified cellulose-based carrier may be correlated with lower costs of process thanks to higher enzyme’s reusability in comparison to unbound enzyme. Moreover, data presented in the current study may serve as proof of a concept of cellulose-based carrier utilization for immobilization of enzymes other than LU and of high industrial importance. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s12010-018-2816-1) contains supplementary material, which is available to authorized users.
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spelling pubmed-63269992019-01-25 Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization Drozd, Radosław Szymańska, Magdalena Rakoczy, Rafał Junka, Adam Szymczyk, Patrycja Fijałkowski, Karol Appl Biochem Biotechnol Article Bacterial cellulose spheres subjected to amination and inlaid modification with superparamagnetic molecules were analyzed with regard to possibility of their application as an immobilization carrier of Lecitase® Ultra (LU) enzyme. The starting point to obtain the carrier was synthesis of bacterial cellulose spheres performed in shaking cultures of Komagataeibacter xylinus. These spheres were subsequently subjected to a multi-stage modification to increase the efficiency of the immobilization process and to separate product from the reaction medium. Maximal yield of Lecitase® Ultra immobilization equaled 70%. It was also found that immobilization process did not affect the pH and LU temperature optimum. Moreover, immobilized enzyme exhibited similar temperature stability profile as its native form. The immobilization process did not significantly affect the enzyme K(M) value. The immobilized enzyme retained over 70% of its initial activity after 8 cycles of use. The immobilized enzyme displayed good storage stability and retained 80% of its initial activity after 4 weeks at 4 °C. The potential application of such modified cellulose-based carrier may be correlated with lower costs of process thanks to higher enzyme’s reusability in comparison to unbound enzyme. Moreover, data presented in the current study may serve as proof of a concept of cellulose-based carrier utilization for immobilization of enzymes other than LU and of high industrial importance. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s12010-018-2816-1) contains supplementary material, which is available to authorized users. Springer US 2018-06-18 2019 /pmc/articles/PMC6326999/ /pubmed/29911267 http://dx.doi.org/10.1007/s12010-018-2816-1 Text en © The Author(s) 2018 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Article
Drozd, Radosław
Szymańska, Magdalena
Rakoczy, Rafał
Junka, Adam
Szymczyk, Patrycja
Fijałkowski, Karol
Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization
title Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization
title_full Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization
title_fullStr Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization
title_full_unstemmed Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization
title_short Functionalized Magnetic Bacterial Cellulose Beads as Carrier for Lecitase® Ultra Immobilization
title_sort functionalized magnetic bacterial cellulose beads as carrier for lecitase® ultra immobilization
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6326999/
https://www.ncbi.nlm.nih.gov/pubmed/29911267
http://dx.doi.org/10.1007/s12010-018-2816-1
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