## Abstract A monofunctional catalase from __Serratia marcescens__ SYBC08 produced by liquid state fermentation in 7 liter fermenter was isolated and purified by ammonium sulfate precipitation (ASP), ion exchange chromatography (IEC), and gel filtration (GF) and characterized. Its sequence was anal
Molecular characterization of polyphosphate (PolyP) operon from Serratia marcescens
โ Scribed by Seung-Jin Lee; Yong-Seok Lee; Young-Choon Lee; Yong-Lark Choi
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 213 KB
- Volume
- 46
- Category
- Article
- ISSN
- 0233-111X
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โฆ Synopsis
The polyphosphate (polyP) operon was cloned from a genomic library of Serratia marcescens KCTC 2172 by Southern hybridization using E. coli ppk gene as a probe. The polyP operon was composed of a polyphosphate promoter, polyphosphate kinase (ppk) and exopolyphosphatase (ppx). A potential CRP binding site and pho box sequence were found in the region upstream of the putative promoter in the regulatory region. The ppk gene comprises 2,063 nucleotides and encodes 686 amino acids yielding a protein with a molecular mass of 70 kDa. The ppx gene contains 1611 nucleotides and encodes 536 amino acids with a molecular 58 kDa. An E. coli strain transformed with the ppk gene had a 16-fold increased in polyphosphate kinase activity, while introduction of the ppx gene produced a 25-fold increase in polyphosphatase activity. E. coli strains transformed with ppk and ppx genes also displayed increased accumulation of polyphosphate.
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