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Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels

Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON M5S 3E5, Canada
Department of Physical and Environmental Sciences, University of Toronto Scarborough, 1065 Military Trail, Scarborough, ON M1C 1A4, Canada
Department of Chemistry, University of Toronto, 80 St. George Street, Toronto, ON M5S 3H6, Canada
Author to whom correspondence should be addressed.
Academic Editors: Francesca D’Anna, Salvatore Marullo and Carla Rizzo
Molecules 2019, 24(16), 2884;
Received: 3 July 2019 / Revised: 25 July 2019 / Accepted: 5 August 2019 / Published: 8 August 2019
(This article belongs to the Special Issue Supramolecular Gel)
PDF [4493 KB, uploaded 16 August 2019]


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. View Full-Text
Keywords: amino acids; protein; hydrogels; enzyme entrapment amino acids; protein; hydrogels; enzyme entrapment

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Falcone, N.; Shao, T.; Rashid, R.; Kraatz, H.-B. Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels. Molecules 2019, 24, 2884.

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