Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels
AbstractSupramolecular 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
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Falcone, N.; Shao, T.; Rashid, R.; Kraatz, H.-B. Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels. Molecules 2019, 24, 2884.
Falcone N, Shao T, Rashid R, Kraatz H-B. Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels. Molecules. 2019; 24(16):2884.Chicago/Turabian Style
Falcone, Natashya; Shao, Tsuimy; Rashid, Roomina; Kraatz, Heinz-Bernhard. 2019. "Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels." Molecules 24, no. 16: 2884.
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