Gene Cloning and Characterization of Thermostable Peptidyl Prolyl cis-trans Isomerase (PPIase) from Bacillus stearothermophilus SIC1
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概要
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The peptidyl prolyl cis-trans isomerase (PPIase, EC 5.2.1.8) gene (ppiT) from Bacillus stearothermophilus SIC1 was cloned on the basis of a partial amino acid sequence of the purified enzyme. ppiT was found as an open reading frame (501 bases) which coded for a protein consisting of 167 amino acid residues (molecular weight, 18,349) (GenBank accession number D42050). The cloned ppiT was overexpressed in Escherichia coli cells using pET-8c as an expression vector. The enzyme was purified by heat treatment and column chromatography on DEAE-Sepharose CL-6B. Purification was about 148-fold and the molecular weight of the enzyme was estimated to be about 18.0 kDa by SDS-PAGE. PPIase activity was determined using synthetic peptide as a substrate in a 2-step peaction coupled with chymotrypsin treatment. The enzyme was stable at pH 7.5-8.0. No heat denaturation was observed when the enzyme was treated at 60℃ for 30 min. The PPIase purified from recombinant E. coli has almost the same characteristics as than from B. stearothermophilus SIC1. In refolding solution, the PPIase enhanced the isomerization rate of unfolded RNase T1.
- 公益社団法人日本生物工学会の論文
- 1995-02-25
著者
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TAKAGI MASAHIRO
Department of Biotechnology, Graduate School of Engineering, Osaka University
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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Morikawa Masaaki
Department Of Biotechnology Department Of Material & Life Science Graduate School Of Engineering
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Kim Dong-ju
Department Of Biotechnology Faculty Of Engineering Osaka University
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Takagi Masahiro
Department Of Biotechnology Faculty Of Engineering Osaka University
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