Structural stability of E. coli transketolase to temperature and pH denaturation

• Transketolase inactivation by pH and temperature is investigated. • Moderate heating initially improves enzyme activity. • Inactivation at low pH and high temperature is caused by irreversible denaturation and aggregation. • High pH affects only the apo-transketolase structure, and is only partial...

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Veröffentlicht in:	Journal of biotechnology 2011-09, Vol.155 (2), p.209-216
Hauptverfasser:	Jahromi, Raha R.F., Morris, Phattaraporn, Martinez-Torres, Ruben J., Dalby, Paul A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biocatalysis Bioconversions. Hemisynthesis Biological and medical sciences Biotechnology Circular Dichroism Denaturation Enzyme Stability Escherichia coli Escherichia coli - enzymology Fluorescence Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Methods. Procedures. Technologies Models, Molecular Particle Size Protein Denaturation Protein Engineering - methods Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Stability Temperature Transketolase Transketolase - isolation & purification Transketolase - metabolism Tryptophan fluorescence
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