کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1386629 | 982520 | 2011 | 10 صفحه PDF | دانلود رایگان |
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.
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Journal: Carbohydrate Polymers - Volume 84, Issue 3, 17 March 2011, Pages 1182–1191