Increased Enzyme Shelf-Life by Encapsulation in Peptide-Based Materials

Peptide-based nanomaterials that protect enzymes over time leading to increased shelf-life.

Enzymes are naturally susceptible to environmental changes resulting in their denaturation and loss of activity, thus rendering them less practical for everyday applications. The main objective is the improvement and increase in enzyme shelf-life thereby allowing their practical use in various daily applications.

We have developed an encapsulation system for enzymes to provide them with support and protection thereby increasing their stability. The enzyme carriers are based on short aromatic peptides capable of forming various structures while encapsulating the enzymes and protecting them. The peptides are biocompatible and biodegradable making them environmentally friendly carriers. By changing the peptides sequences, different morphologies, such as nanospheres, may be obtained (Figure 1A, B). These peptide structures are non-specific for a particular enzyme family thus allowing the entrapment of different enzymes for their long-term protection (Figure 1C).

Figure 1: Encapsulation of enzymes in BocFF spheres. (A) Molecular structure of the BocFF peptide. (B) Scanning electron microscopy images of peptide nanospheres. (C) Confocal microscopy images of labeled enzymes encapsulated in BocFF spheres. Left: optical image; Center: a fluorescence image; Right: a merged image showing the encapsulation of the labeled enzyme inside the spheres. 

1. Enzyme protection platform: Different enzymes may be encapsulated allowing their activity over time.
2. Enzyme mediated antibacterial treatment.

As verified by in vitro and in vivo assays, the encapsulation of the enzymes resulted in increased shelf-life of the enzymes over an extended period of time, in contrast to their free counterparts. The use of different peptides and assembly conditions allows to control the structures shapes while still maintaining enzyme protection capabilities. Moreover, various enzymes derived from different families could be entrapped within the structures as well as stabilized by them. We have recently shown the encapsulation and protection of parathion hydrolase from the acyl-homoserine lactonase family, and its use against a plant pathogen as an antibacterial treatment.

US Provisional Patent.

Directed Enzyme Evolution and Encapsulation in Peptide Nanospheres of Quorum Quenching Lactonase as an Antibacterial Treatment against Plant Pathogen, ACS Appl. Mater. Interfaces 2021, 13, 2, 2179–2188. https://doi.org/10.1021/acsami…

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