Korean Journal of Fisheries and Aquatic Sciences (한국수산과학회지)
- Volume 28 Issue 6
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- Pages.728-735
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- 1995
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- 0374-8111(pISSN)
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- 2287-8815(eISSN)
Purification and Characterization of Peptidyl Prolyl cis-trans Isomerase (PPlase) from Bacillus stearothermophilus SIC1
Abstract
The peptidyl prolyl cis-trans isomerase(PPlase, EC 5.2.2.8) from Bacillus stearothermophilus SIC1 was extracted from the cells treated with by lysozyme. PPlase was purified from the cell extracts by heat treatment, ammonium sulfate precipitation, ion exchange chromatography and finally gel filtration (FPLC). The purity of purified the enzyme after Superose 12 column chromatography was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE). The molecular weight of the purified PPlase was estimated as 18,000 by SDS-PAGE. The 39 amino acid residues from the N-terminus were determined by the protein sequencer. The enzyme showed the optimum pH at 8.0 and was stable at the range of pH 7.0 to 8.0. The enzyme was considerably stable after heat treatment at