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Spore Adsorption as a Nonrecombinant Display System for Enzymes and Antigens

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Spore-displayed enzyme cascade with tunable stoichiometry.

Long Chen¹, Ashok Mulchandani¹, Xin Ge¹

¹Dept. of Chemical and Environmental Engineering, University of California, Riverside, CA, 92521.

Biotechnology Progress

|December 16, 2016

Summary

This summary is machine-generated.

This study developed a biocatalysis platform using Bacillus subtilis endospores for immobilizing multiple enzymes. This novel approach enhances enzyme stability and allows controllable stoichiometry for improved xylitol production.

Keywords:

cofactor regeneration cohesin-dockerin interaction enzyme cascade enzyme immobilization spore surface display

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Area of Science:

Biocatalysis and enzyme immobilization
Biotechnology and metabolic engineering
Surface display technologies

Background:

Endospores offer a stable and inert platform for biocatalysis.
Enzyme cascade immobilization is crucial for efficient multi-step biotransformations.
Controlling enzyme ratios is key to optimizing reaction yields.

Purpose of the Study:

To develop a novel biocatalysis platform using Bacillus subtilis endospore surfaces for enzyme immobilization.
To demonstrate the co-immobilization of multiple enzymes for cascade reactions.
To investigate the impact of tunable enzyme stoichiometry on product yield.

Main Methods:

Utilized Bacillus subtilis spores for surface display of enzymes via outer coat proteins (CotG).
Engineered fusion proteins of enzymes (xylose reductase, phosphite dehydrogenase) with cohesin-dockerin modules for immobilization.
Co-immobilized enzymes using different cohesin-dockerin pairs (Clostridium thermocellum, Ruminococcus flavefaciens).
Adjusted enzyme stoichiometry by altering the copy numbers of displayed cohesin modules.

Main Results:

Achieved high-level functional display of enzymes (∼10^4 molecules per spore) on the endospore surface.
Demonstrated enhanced stability of immobilized enzymes (xylose reductase, phosphite dehydrogenase).
Successfully regenerated NADPH using co-immobilized phosphite dehydrogenase.
Optimized enzyme stoichiometry led to increased xylitol yields.

Conclusions:

Endospore surface display is a viable and novel approach for enzyme cascade immobilization.
This method provides improved enzyme stability and controllable stoichiometry.
The platform offers a promising strategy for enhancing biocatalytic processes.