Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels.

Falcone Falcone,Shao Shao,Kraatz Kraatz,Rashid Rashid

doi:10.3390/molecules24162884

Falcone Falcone, Shao Shao + Show 2 more

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https://doi.org/10.3390/molecules24162884

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Abstract

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.

Highlights

Amino acid and peptide-based supramolecular gels are functional materials that have been the subject of research due to their versatility and their wide range of applications in many fields [1]
Supramolecular amino acid and peptide hydrogels formed by self-assembly of amphiphilic molecules have served as scaffolds for tissue engineering and wound healing [4,5], mediums for environmental remediation [6,7], biomaterials for drug delivery, and as antimicrobial agents [8,9,10], their applications as matrices for enzymatic reactions to occur in have been rarely explored
Molecules 2019, 24, 2884 transmission electron microscopy (TEM) studies was compared. It is shown in the circular dichroism (CD) spectrum that the Phe compound was found to form an ordered structure exhibiting a distinct ultra-narrow peak around 220–230 nm, which attributes to the formation of Phe-based chiral structures that correspond to structural aggregates. Both hydrogels were tested for entrapment capabilities with two common and significant enzymes: Horseradish peroxidase (HRP) and α-amylase

Summary

Introduction

Amino acid and peptide-based supramolecular gels are functional materials that have been the subject of research due to their versatility and their wide range of applications in many fields [1]. Interactions generating the supramolecular network present in physical gels are the result of non-covalent interactions between gelator molecules. Non-covalent interactions present in amino acid and peptide gel materials include hydrogen bonding, van der Waals interactions, π−π stacking, and hydrophobic interactions. In industrial biotransformations, using enzymes as biocatalysts are attractive as they possess high selectivity, run under milder and greener reaction conditions, and eliminate the need of expensive and toxic metal catalysts [11]. Enzymes are attractive “green” alternatives to chemical catalysts within the industrial sector, but their robustness to environmental conditions needs optimizing. There are three main immobilization methods: Adsorption [12], entrapment [13], and covalent bonding (Scheme 1) [14]

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