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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Main Authors: Natashya Falcone, Tsuimy Shao, Roomina Rashid, Heinz-Bernhard Kraatz
Format: Article
Language:English
Published: MDPI AG 2019-08-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/24/16/2884
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spelling 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
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