Characterization of hyaluronate lyase from Streptococcus pyogenes bacteriophage H4489A

Nermeen S. El-Safory, Guan Chiun Lee, Cheng Kang Lee

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7 Citations (Scopus)


Hyaluronate (HA) lyase of Streptococcus pyogenes bacteriophage H4489A, was expressed in Escherichia coli, purified, and characterized. The purified homogeneous preparation of HA lyase had a molecular mass of 40 kDa. The optimum enzymatic activity was achieved at pH ∼ 5.5 and 37 °C, and the enzyme was stable at pH profile from 4 to 7 and temperature range from 25 to 45 °C. The enzymatic activity was vaguely enhanced by Mg2+, slightly inhibited by Ca2+, triton X-100, and Tween 80, strongly inhibited by Zn2+, and completely inhibited by Cu2+, Ni2+, Co2+ and sodium dodecyl sulfate. Kinetic measurements give Michaelis constant of 0.44 mg/ml, maximal velocity of 0.20 μmol ml-1 min-1, and showed that bacteriophage HA lyase degraded the HA efficiently. Light scattering dynamic measurements determined the denaturation temperate of HA lyase of about 46 °C. Circular dichromism and UV-visible absorption spectroscopy estimated the changes in secondary structure of native and denatureated HA lyase.

Original languageEnglish
Pages (from-to)1182-1191
Number of pages10
JournalCarbohydrate Polymers
Issue number3
Publication statusPublished - 2011 Mar 17


  • Characterization
  • Hyaluronate lyase
  • Kinetics
  • Purification
  • Structure

ASJC Scopus subject areas

  • Organic Chemistry
  • Polymers and Plastics
  • Materials Chemistry


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