Development of a peroxidase-Fused protein reagent by brevibacillus choshinensis heterologous expression system

Kounosuke Hayashi, Yusuke Tomozoe, Kenji Nagai, Yoshiyuki Hiraishi, Noriho Kamiya

研究成果: ジャーナルへの寄稿学術誌査読

抄録

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.

本文言語英語
ページ(範囲)157-161
ページ数5
ジャーナルkagaku kogaku ronbunshu
41
2
DOI
出版ステータス出版済み - 3月 20 2015

!!!All Science Journal Classification (ASJC) codes

  • 化学 (全般)
  • 化学工学(全般)

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