Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii

The purification and characterization of intracellular tyrosine phenol lyase from Citrobacter freundii has been carried out. The enzyme was purified 35-fold to homogeneity by ammonium sulphate precipitation and hydrophobic interaction chromatography. Its subunit molecular weight was found to be 52 k...

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Veröffentlicht in:	Applied biochemistry and biotechnology 2013-12, Vol.171 (8), p.2040-2052
Hauptverfasser:	Chandel, Meenakshi, Azmi, Wamik
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence amino acid sequences Amino acids Ammonium ammonium sulfate Biochemistry Biological and medical sciences Biotechnology carbon-carbon lyases Chemistry Chemistry and Materials Science Chromatography Citrobacter freundii Citrobacter freundii - enzymology Dipeptides - chemistry Enzymes Fundamental and applied biological sciences. Psychology hydrophobic bonding Kinetics Molecular Weight phenol Phenols polyacrylamide gel electrophoresis sodium dodecyl sulfate Sulfates tyrosine Tyrosine Phenol-Lyase - chemistry Tyrosine Phenol-Lyase - isolation & purification
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