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  • Title: [Purification and properties of a thermostable chitinase from thermophilic fungus Thermomyces lanuginosus].
    Author: Guo RF, Li DC, Wang R.
    Journal: Wei Sheng Wu Xue Bao; 2005 Apr; 45(2):270-4. PubMed ID: 15989274.
    Abstract:
    A thermostable extracellular chitinase from culture supernatant of a thermophilic fungus Thermomyces lanuginosus was purified to SDS-PAGE homogeneity, by using ammonium sulfate fraction, DEAE-Sepharose Fast flow chromatography, Phenyl-Sepharose Fast Flow chromatography. A molecular mass of the purified enzyme was between 48-49.8 kD determined by SDS-PAGE and gel filtration chromatography. The chitinase exhibited optimum catalytic activity at pH 4.5 and 55 degrees C respectively. It was thermostable at 50 degrees C and retained 24% activity after 20 min at 70 degrees C. The half life time of the enzyme at 65 degrees C was 25 min. Different metal ions showed different effects on the chitinase activity. Ca2+, Ba2+, Na+, K+ enhanced the enzyme activity, whereas Fe2+, Ag+, Hg2+, Cu2+ caused obvious inhibition. The Km and Vmax values of chitinase on colloidal chitin were 9.56 mg/mL and 22.12 micromol/min respectively. The chitinase showed antifungal activity aginst tested fungi to different degree.
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