Development of a Peroxidase-Fused Protein Reagent by <i>Brevibacillus choshinensis</i> Heterologous Expression System

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  • ブレビバチルス発現系によるペルオキシダーゼ融合タンパク質試薬の調製
  • ブレビバチルス ハツゲンケイ ニ ヨル ペルオキシダーゼ ユウゴウ タンパクシツ シヤク ノ チョウセイ

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To detect a target protein in biological samples, a fusion protein was designed composed of a peroxidase from Arthromyces ramosus (ARP) and parts of the antibody-binding domains of Staphylococcus aureus protein A and Streptococcus protein G (PG). The ARP-PG fusion protein was successfully expressed by a heterologous protein expression system in Brevibacillus choshinensis. The fusion protein was secreted as an active form in culture media. The production of ARP-PG with higher peroxidase activity was observed by the addition of 5-aminolevulinic acid to the culture media. The performance of purified ARP-PG was validated by dot blotting for the detection of transferrin as a model target protein. A comparable performance in the dot blot analysis was attained using a culture supernatant containing crude but active ARP-PG, indicating the practicality of the Brevibacillus protein secretion system.

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