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Tagging and Fusion Proteins

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Microfluidic On-chip Capture-cycloaddition Reaction to Reversibly Immobilize Small Molecules or Multi-component Structures for Biosensor Applications

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Non-covalent binding tags for batch and flow biocatalysis.

Raquel A Rocha¹, Lygie Esquirol², Vivien Rolland³

¹School of Biology and Environmental Science, Faculty of Science, Queensland University of Technology (QUT), Brisbane, Qld 4000, Australia; CSIRO Environment, Black Mountain Science and Innovation Park, Canberra, ACT 2601, Australia.

Enzyme and Microbial Technology

|June 10, 2023

Summary

New enzyme immobilization methods use specific binding tags for cellulose and silica carriers. This approach simplifies enzyme attachment, enabling efficient biocatalysis in batch and continuous flow systems.

Keywords:

Carbohydrate binding domain Continuous flow reactors Enzyme immobilization Modularity Process design Silicon binding tag

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Area of Science:

Biocatalysis and Enzyme Engineering
Biotechnology and Protein Chemistry

Background:

Enzyme immobilization enhances biocatalysis but often requires costly chemical modification of carriers.
Existing immobilization methods lack specificity and can increase processing costs.

Purpose of the Study:

To investigate novel enzyme immobilization strategies using specific binding tags on cellulose and silica carriers.
To evaluate the performance of industrially relevant enzymes (transaminases, imine reductase/glucose oxidoreductase fusion) after immobilization.

Main Methods:

Fusing known binding tags (Bacillus cereus CotB peptide, Clostridium thermocellum cellulose binding domain) to model and industrial proteins.
Assessing binding affinity (K_d values) and enzyme activity post-immobilization on respective carriers.
Testing immobilized enzymes in repetitive batch and continuous-flow reactors.

Main Results:

Both binding tags demonstrated high-affinity, specific binding to their respective carriers (cellulose and silica).
The silica-binding peptide caused protein aggregation, while the cellulose-binding domain allowed immobilization but caused activity loss in some enzymes.
A transaminase-cellulose binding domain fusion was successfully applied in both batch and continuous-flow reactors.

Conclusions:

Specific binding tags offer a cost-effective alternative to chemical modification for enzyme immobilization.
The cellulose-binding domain (CBDclos) shows promise for enzyme immobilization in flow chemistry, despite initial activity challenges.
This study demonstrates the potential of engineered binding tags for simplified and efficient enzyme immobilization in industrial biocatalysis.