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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2025.3
- 수록면
- 81 - 86 (6page)
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We demonstrated surface expression of trehalose synthase from Pseudomonas putida using YiaT outer membrane as an anchoring motif on the Escherichia coli and bio-conversion of maltose to trehalose via newly developed whole-cell enzyme. Localization of trehalose synthase on the cell surface was verified by measuring whole cell activity, western blot analysis, and immunofluorescence microscopy. Conversion yield was obtained 36.0% under the optimized conditions of pH 8.00 and 30oC, 24 h reaction time, and 10 g/L of maltose, and surface displayed TreS maintained over 59% of initial activity after consecutive 10 repeated reactions. These results suggested that trehalose synthase from P. putida was successfully expressed on the surface of E. coli via C-terminal deletion fusion with YiaT anchoring motif and TreS displayed E. coli can be used for the whole-cell production of trehalose.
목차
Abstract
1. INTRODUCTION
2. MATERIALS AND METHODS
3. RESULTS AND DISCUSSION
4. DISCUSSION
REFERENCES
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