초고온성 아케아 써모코커스 NA1의 녹말분해효소의 과발현 및 특성
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Title
- 초고온성 아케아 써모코커스 NA1의 녹말분해효소의 과발현 및 특성
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Alternative Title
- Overexpression and characterization of an alpha amylase from the hyperthermophilic archaeon THermococcus sp. NA1
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Author(s)
- 임재규; 이현숙; 김윤재; 전정호; 이규호; 강성균; 이정현
- KIOST Author(s)
- Lim, Jae Kyu(임재규); Lee, Hyun Sook(이현숙); Kim, Yun Jae(김윤재); Kang, Sung Gyun(강성균); Lee, Jung Hyun(이정현)
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Alternative Author(s)
- 임재규; 이현숙; 김윤재; 전정호; 강성균; 이정현
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Publication Year
- 2005-10-13
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Abstract
- Genomic analysis of a hyperthermophilic archaeon Thermococcus NA1. revealed the presence of an open reading frame consisting of 1,377 bp similar to GH13 a-amylases from the genus Thermococcus and Pyrococcus. This amylolytic enzyme, designated TNA1_amyl (Thermococcus sp. NA1 amylase), was cloned and expressed in Escherichia coli. The full-length protein was detected in the culture supernatant, indicating that the signal peptide was processed in E. coli and thus the mature form of the protein was reconstructed based on N-terminal sequencing data of the secreted recombinant protein. The purified protein by His-tagged affinity chromatography was highly thermostable with an optimum temperature of 80°C, and an optimum pH of 5.5. More than 50% of the maximum activity was retained in the range between pH 5.0 and pH 9.5. The enzyme displayed thermostability with half-life (t1/2) of 10 min at 90°C, and the thermostability of TNA1_amyl was significantly enhanced in the presence of calcium with half-life (t1/2) of 153 min at 90°C. TNA1_amyl hydrolyzed maltooligosaccharides, amylopectin and starch, not pullulan to produce mainly G2 to G7.
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/31297
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Bibliographic Citation
- 한국미생물연합회 프로시딩, pp.263, 2005
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Publisher
- 한국미생물연합회
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Type
- Conference
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Language
- English
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