초고온성 아케아 써모코커스 NA1의 녹말분해효소의 과발현 및 특성

Title
초고온성 아케아 써모코커스 NA1의 녹말분해효소의 과발현 및 특성
Alternative Title
Overexpression and characterization of an alpha amylase from the hyperthermophilic archaeon THermococcus sp. NA1
Author(s)
임재규; 이현숙; 김윤재; 전정호; 이규호; 강성균; 이정현
KIOST Author(s)
Lee, Hyun Sook(이현숙)Kang, Sung Gyun(강성균)Lee, Jung Hyun(이정현)
Publication Year
2005-10-13
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.
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/31297
Bibliographic Citation
한국미생물연합회 프로시딩, pp.263, 2005
Publisher
한국미생물연합회
Type
Conference
Language
English
Publisher
한국미생물연합회
Related Researcher
Research Interests

marine biotechnology,molecular microbiology,해양생명공학,분자미생물학

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