Bacillus subtilis AprX involved in degradation of a heterologous protein during the late stationary growth phase

Takeko Kodama, Keiji Endo, Kazuhisa Sawada, Katsutoshi Ara, Katsuya Ozaki, Hiroshi Kakeshita, Kunio Yamane, Junichi Sekiguchi*

*この研究の対応する著者

研究成果: Article査読

19 被引用数 (Scopus)

抄録

In Bacillus subtilis, extracellular protease-deficient mutants have been used in attempts to increase the productivity of heterologous proteins. We detected protease activity of AprX using protease zymography in the culture medium at the late stationary growth phase. An α-amylase-A522-PreS2 hybrid protein, in which the PreS2 antigen of human hepatitis B virus (HBV) is fused with the N-terminal 522-amino-acid polypeptide of B. subtilis α-amylase, has been produced in multiple-protease-deficient mutants. The B. subtilis KA8AX strain, which is deficient in eight extracellular proteases and AprX, did not show the proteolysis of α-amylase-A522-PreS2 in the late stationary growth phase. Moreover, the production of α-amylase-A522-PreS2 was about 80 mg/l, which was eight times higher than that by the KA8AX strain previously reported. In addition, we showed the degradation of the heterologous protein by AprX that leaked to the culture medium (probably caused by cell lysis) during the late stationary growth phase.

本文言語English
ページ(範囲)135-143
ページ数9
ジャーナルJournal of Bioscience and Bioengineering
104
2
DOI
出版ステータスPublished - 2007 8月
外部発表はい

ASJC Scopus subject areas

  • バイオテクノロジー
  • バイオエンジニアリング
  • 応用微生物学とバイオテクノロジー

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