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Updated: May 29, 2026

Spore Adsorption as a Nonrecombinant Display System for Enzymes and Antigens
Published on: March 19, 2019
Bacterial surface display of a co-factor containing enzyme, ω-transaminase from Vibrio fluvialis using the Bacillus
Bum-Yeol Hwang1, Byung-Gee Kim, June-Hyung Kim
1Department of Chemical Engineering and Bioengineering and The Helen Wills Neuroscience Institute, University of California, Berkeley, CA 94720-3220, USA.
Abstract:
To improve the conventional bacterial surface display systems and to display a co-factor containing enzyme, ω-transaminase from Vibrio fluvialis, which needs pyridoxal phosphate (PLP) for efficient transamination, Bacillus subtilis spore display system with cotG, as an anchoring motif was used. Flow cytometry of the B. subtilis spore-expressing ω-transaminase proved its surface localization on the spore. The enzymatic activity of the spore expressing ω-transaminase was more than 30 times higher than that of the host spore. Protease treatment of the ω-transaminase displaying spores resulted in decreased transaminase activity, which is in keeping with the surface location of the fusion protein, CotG-ω-transaminase.
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