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Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels

Supramolecular amino acid and peptide hydrogels are functional materials with a wide range of applications, however, their ability to serve as matrices for enzyme entrapment have been rarely explored. Two amino acid conjugates were synthesized and explored for hydrogel formation. These hydrogels wer...

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Detalles Bibliográficos
Autores principales: Falcone, Natashya, Shao, Tsuimy, Rashid, Roomina, Kraatz, Heinz-Bernhard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721053/
https://www.ncbi.nlm.nih.gov/pubmed/31398913
http://dx.doi.org/10.3390/molecules24162884
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author Falcone, Natashya
Shao, Tsuimy
Rashid, Roomina
Kraatz, Heinz-Bernhard
author_facet Falcone, Natashya
Shao, Tsuimy
Rashid, Roomina
Kraatz, Heinz-Bernhard
author_sort Falcone, Natashya
collection PubMed
description Supramolecular amino acid and peptide hydrogels are functional materials with a wide range of applications, however, their ability to serve as matrices for enzyme entrapment have been rarely explored. Two amino acid conjugates were synthesized and explored for hydrogel formation. These hydrogels were characterized in terms of strength and morphology, and their ability to entrap enzymes while keeping them active and reusable was explored. It was found that the hydrogels were able to successfully entrap two common and significant enzymes—horseradish peroxidase and α-amylase—thus keeping them active and stable, along with inducing recycling capabilities, which has potential to further advance the industrial biotransformation field.
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spelling pubmed-67210532019-09-10 Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels Falcone, Natashya Shao, Tsuimy Rashid, Roomina Kraatz, Heinz-Bernhard Molecules Article Supramolecular amino acid and peptide hydrogels are functional materials with a wide range of applications, however, their ability to serve as matrices for enzyme entrapment have been rarely explored. Two amino acid conjugates were synthesized and explored for hydrogel formation. These hydrogels were characterized in terms of strength and morphology, and their ability to entrap enzymes while keeping them active and reusable was explored. It was found that the hydrogels were able to successfully entrap two common and significant enzymes—horseradish peroxidase and α-amylase—thus keeping them active and stable, along with inducing recycling capabilities, which has potential to further advance the industrial biotransformation field. MDPI 2019-08-08 /pmc/articles/PMC6721053/ /pubmed/31398913 http://dx.doi.org/10.3390/molecules24162884 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
Falcone, Natashya
Shao, Tsuimy
Rashid, Roomina
Kraatz, Heinz-Bernhard
Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels
title Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels
title_full Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels
title_fullStr Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels
title_full_unstemmed Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels
title_short Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels
title_sort enzyme entrapment in amphiphilic myristyl-phenylalanine hydrogels
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721053/
https://www.ncbi.nlm.nih.gov/pubmed/31398913
http://dx.doi.org/10.3390/molecules24162884
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