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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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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. |
format | Online Article Text |
id | pubmed-6721053 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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