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Novel Highly Active Recombinant Glutaredoxin from Chlorella sorokiniana T-89

By Hsu-Han Chuang, Chu-Ying Cheng, Yu-Ting Chen and Jei-Fu Shaw


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

Topics: 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
Year: 2015
DOI identifier: 10.1021/jf405213h
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