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The article presents a study that evaluates the bacterial surface display of w-transminase as a co-factor for efficient transamination and is functional in the dimeric state. The study is undertaken through constructing CotG-w-TA fusion protein expression by double digested polymerase chain reaction (PCR) product and through the use of protease accessibility test. The results of the study show a successful display of co-factor containing, which consists phosphate, and dimer-forming enzyme.

Abstract: Streptavidin, which is one of the most widely used proteins in biotechnological application field and is active only in tetrameric form, was surface expressed on the surface of Bacillus subtilis spore. Spore coat protein of B. subtilis, CotG, was used as an anchoring motif to display streptavidin. FACS using anti-streptavidin antibody was used for the verification of surface localization of expressed CotG-streptavidin fusion protein. FACS and dot-blot were used for the verification of biological activity of displayed streptavidin with FITC-labeled biotin. [Copyright &y& Elsevier]