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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Online Access: | https://www.mdpi.com/1420-3049/24/16/2884 |
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doaj-cce71e7cfb284ab0880ff402e319dbe62020-11-25T01:57:18ZengMDPI AGMolecules1420-30492019-08-012416288410.3390/molecules24162884molecules24162884Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine HydrogelsNatashya Falcone0Tsuimy Shao1Roomina Rashid2Heinz-Bernhard Kraatz3Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON M5S 3E5, CanadaDepartment of Physical and Environmental Sciences, University of Toronto Scarborough, 1065 Military Trail, Scarborough, ON M1C 1A4, CanadaDepartment of Physical and Environmental Sciences, University of Toronto Scarborough, 1065 Military Trail, Scarborough, ON M1C 1A4, CanadaDepartment of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON M5S 3E5, CanadaSupramolecular 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.https://www.mdpi.com/1420-3049/24/16/2884amino acidsproteinhydrogelsenzyme entrapment |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Natashya Falcone Tsuimy Shao Roomina Rashid Heinz-Bernhard Kraatz |
spellingShingle |
Natashya Falcone Tsuimy Shao Roomina Rashid Heinz-Bernhard Kraatz Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels Molecules amino acids protein hydrogels enzyme entrapment |
author_facet |
Natashya Falcone Tsuimy Shao Roomina Rashid Heinz-Bernhard Kraatz |
author_sort |
Natashya Falcone |
title |
Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels |
title_short |
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_sort |
enzyme entrapment in amphiphilic myristyl-phenylalanine hydrogels |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2019-08-01 |
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. |
topic |
amino acids protein hydrogels enzyme entrapment |
url |
https://www.mdpi.com/1420-3049/24/16/2884 |
work_keys_str_mv |
AT natashyafalcone enzymeentrapmentinamphiphilicmyristylphenylalaninehydrogels AT tsuimyshao enzymeentrapmentinamphiphilicmyristylphenylalaninehydrogels AT roominarashid enzymeentrapmentinamphiphilicmyristylphenylalaninehydrogels AT heinzbernhardkraatz enzymeentrapmentinamphiphilicmyristylphenylalaninehydrogels |
_version_ |
1724974833602658304 |