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 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 -amylase—thus keeping them active and stable, along with inducing recycling capabilities, which has potential to further advance the industrial biotransformation field

Systematic Exploration of the pH-dependence of a peptide hydrogel

Stimuli-responsive peptide gels are a growing class of functional biomaterials that are involved in many applications in research. Here, we present a novel di-peptide hydrogel from the compound Boc-Phe-Trp-OH in various buffer and pH conditions. We examine the effects of different stimuli including temperature and pH on the mechanical strength of the gels through frequency rheology studies. We found that this hydrogelator is highly pH dependent only forming a gel in a narrow range of pH 6-7. This hydrogelator hold promise for the development of new stimuli-responsive biomaterials for specific applications that require this type of specific stimuli.The accepted manuscript in pdf format is listed with the files at the bottom of this page. The presentation of the authors' names and (or) special characters in the title of the manuscript may differ slightly between what is listed on this page and what is listed in the pdf file of the accepted manuscript; that in the pdf file of the accepted manuscript is what was submitted by the author

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 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