Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane

Two commercially available enzymes, Dextrozyme (α-amylase) and Esperase (protease), were covalently immobilized on non-woven electrospun poly(styrene-co-maleic anhydride) nanofiber mats with partial retention of their catalytic activity. Immobilization was achieved for the enzymes on their own as we...

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Detalles Bibliográficos
Autores principales: Cloete, William J., Hayward, Stefan, Swart, Pieter, Klumperman, Bert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6384644/
https://www.ncbi.nlm.nih.gov/pubmed/30708952
http://dx.doi.org/10.3390/molecules24030508
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author Cloete, William J.
Hayward, Stefan
Swart, Pieter
Klumperman, Bert
author_facet Cloete, William J.
Hayward, Stefan
Swart, Pieter
Klumperman, Bert
author_sort Cloete, William J.
collection PubMed
description Two commercially available enzymes, Dextrozyme (α-amylase) and Esperase (protease), were covalently immobilized on non-woven electrospun poly(styrene-co-maleic anhydride) nanofiber mats with partial retention of their catalytic activity. Immobilization was achieved for the enzymes on their own as well as in different combinations with an additional enzyme, β-galactosidase, on the same non-woven nanofiber mat. This experiment yielded a universal method for immobilizing different combinations of enzymes with nanofibrous mats containing maleic anhydride (MAnh) residues in the polymer backbone.
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spelling pubmed-63846442019-02-23 Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane Cloete, William J. Hayward, Stefan Swart, Pieter Klumperman, Bert Molecules Article Two commercially available enzymes, Dextrozyme (α-amylase) and Esperase (protease), were covalently immobilized on non-woven electrospun poly(styrene-co-maleic anhydride) nanofiber mats with partial retention of their catalytic activity. Immobilization was achieved for the enzymes on their own as well as in different combinations with an additional enzyme, β-galactosidase, on the same non-woven nanofiber mat. This experiment yielded a universal method for immobilizing different combinations of enzymes with nanofibrous mats containing maleic anhydride (MAnh) residues in the polymer backbone. MDPI 2019-01-31 /pmc/articles/PMC6384644/ /pubmed/30708952 http://dx.doi.org/10.3390/molecules24030508 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Cloete, William J.
Hayward, Stefan
Swart, Pieter
Klumperman, Bert
Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane
title Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane
title_full Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane
title_fullStr Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane
title_full_unstemmed Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane
title_short Degradation of Proteins and Starch by Combined Immobilization of Protease, α-Amylase and β-Galactosidase on a Single Electrospun Nanofibrous Membrane
title_sort degradation of proteins and starch by combined immobilization of protease, α-amylase and β-galactosidase on a single electrospun nanofibrous membrane
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6384644/
https://www.ncbi.nlm.nih.gov/pubmed/30708952
http://dx.doi.org/10.3390/molecules24030508
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