Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/86400
標題: Novel Highly Active Recombinant Glutaredoxin from Chlorella sorokiniana T-89
作者: Chuang, Hsu-Han
Cheng, Chu-Ying
Chen, Yu-Ting
Shaw, Jei-Fu
關鍵字: Amino Acid Sequence
Base Sequence
Catalytic Domain
Chlorella
Cloning, Molecular
DNA, Complementary
Enzyme Stability
Escherichia coli
Gene Expression
Glutaredoxins
Hydrogen-Ion Concentration
Infrared Rays
Molecular Sequence Data
Mutagenesis, Site-Directed
Recombinant Proteins
Sequence Alignment
摘要: Glutaredoxin (Grx) is a thiol/disulfide oxidoreductase that maintains the cellular thiol/disulfide ratio. A 321 bp cDNA fragment encoding a putative Grx (named CsT-89Grx) was cloned from heat-tolerant Chlorella sorokiniana T-89 and expressed in an Escherichia coli system. The sequence analysis of CsT-89Grx and site-directed mutations showed that the putative active site within the CPYC motif belonged to the dithiol superfamily. The biochemical property analyses showed that the optimal pH and temperature of CsT-89Grx are pH 8.5 and 50 °C, respectively. The activity of CsT-89Grx showed high thermal stability (retained 70% activity at 80 °C for 30 min) and broad pH stability (retained over 70% activity for 1 h) ranging from pH 3 to 11. The kinetic parameter kcat/Km was 20,982 min(-1) mM(-1), which suggested that CsT-89Grx exhibited the highest catalytic efficiency in reducing the disulfide bond among all the Grx reported in the related literature and is therefore potentially useful for industrial applications.
URI: http://hdl.handle.net/11455/86400
ISSN: 0021-8561
1520-5118
1520-5118
Appears in Collections:基因體暨生物資訊學研究所

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